@article{HackerOttHof1993,
  author    = {Hacker, J{\"o}rg and Ott, M. and Hof, H.},
  title     = {Effects of low, subinhibitory concentrations of antibiotics on expression of a virulence gene cluster of pathogenic E. coli by using a wild-type gene fusion},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59874},
  year      = {1993},
  abstract  = {No abstract available},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{ZinglerBlumFalkenhagenetal.1993,
  author    = {Zingler, G. and Blum, G. and Falkenhagen, U. and Orskov, I. and Orskov, F. and Hacker, J{\"o}rg and Ott, M},
  title     = {Clonal differentiation of uropathogenic E. coli isolates of serotype O6:K5 by fimbrial antigen typing and DNA long-range mapping techniques},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59865},
  year      = {1993},
  abstract  = {Escherichia coli isolates of serotype 06: K5 are the most common causative agents of cystitis and pyelonephritis in adults. To answer the question, as to whether strains of this particular serotype represent one special clonal group, out of a collection of 34 serotype 06: K5 isolates [Zingler et al. ( 1990) Zentralbl. Bakteriol Mikrobiol Hyg [A] 274:372-381] 15 strains were selected andanalyzed in detail. The flagellar (H) antigen and the outer membrane protein (OMP) pattern were determined. Furtherserum resistance properties and the genetic presence and expression of other virulence factors, including hemolysin, aerobactin, P fimbriae, S/F1C fimbriae and type 1 fimbriae was evaluated. In~laddition the Xbalmacrorestriction pattern of ten representative isolates was elaborated and the fimbrial (F) antigentype ofthe P fimbriae was determined, to obtain the complete 0: K: H: F pattern. These analyses could clearly show that the 06: K5 isolates do not represent one clonal group. The Xbal-macrorestriction profiles were heterogeneaus and marked differences in the hybridization patterns, using virulenceassociated gene probes in Southern hybridization of long-range-separated genomic DNA, were observed among the strains. However, some of strains showed similarities in the genomic profiles, arguing for clonal groupings among the 06: K5 isolates. lnterstingly the strains grouped tagether exhibited the same fimbrial F typethat many indicate a coincidence of this phenotypic trait with clonality.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{HackerKestlerHoschuetzkyetal.1993,
  author    = {Hacker, J{\"o}rg and Kestler, H. and Hosch{\"u}tzky, H. and Jann, K. and Lottspeich, F. and Korhonen, T. K.},
  title     = {Cloning and characterization of the S fimbrial adhesin (SfaII) complex of an Escherichia coli O18:K1 meningitis isolate},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59853},
  year      = {1993},
  abstract  = {S fimbrial adbesins (Sfa), which are able to recognize sialic acid-containing receptors on eukaryotic cells, are produced by Escherichia coli strains causing urinary tract infections or newbom meningitis. We recently described tbe cloning and molecular cbaracterization of a determinant, termed sftJI, from the chromosome of an E. coli urinary tract infection strain. Herewe present data conceming a S fimbria-specific gene duster, designated sfall, of an E. coli newbom meningitis strain. Like tbe Sfal complex, Sfall consists of tbe major subunit protein SfaA (16 kDa) and the minor subunit proteins SfaG (17 kDa), SfaS (15 kDa), and SfaH (29 kDa). The genes encoding tbe subunit proteins of Sfall were identified and sequenced. Their protein sequences were calculated from the DNA sequences and compared with tbose of the Sfal complex subunits. Altbough the sequences ofthe two major SfaA subunits ditf'ered markedly, tbe sequences ofthe minor subunits sbowed only a few amino acid exchanges (SfaG, SfaH) or were completely identical (SfaS). The introduction of a site-specific mutation into the gene sfaSII and subsequent analysis of an SfaS-negative clone indicated that sfaSII codes for the sialic acid-specific adhesin of tbe meninigitis isolate. These data were confirmed by tbe isolation and characterization of tbe SfaSII protein and the determination of its N-terminal amino acid sequence. The identity between the sialic acid-specific adhesins of Sfal and Sfall revealed that difl'erences between the two Sfa complexes with respect to tbeir capacities to agglutinate erythrocytes must result from sequence alterations of subunit proteins other tban SfaS.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MorschhaeuserUhlinHacker1993,
  author    = {Morschh{\"a}user, J. and Uhlin, B. E. and Hacker, J{\"o}rg},
  title     = {Transcriptional analysis and regulation of the sfa determinant coding for S fimbria of pathogenic E. coli strains},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59844},
  year      = {1993},
  abstract  = {The sfa determinant codes for S fimbrial adhesins which constitute adherence factors of pathogenic Escherichia coli strains. Wehave recently shown that the sfa determinant is transcribed from three pr{\"o}moters, pA, pB, and pC. In comparison with the promoters pB and pC, promoter pA, which is located in front of the structural gene sfaA, showed very weak activity. Herewe have determined the exact positions ofthe mRNA start points by primer extension studies. We have also shown that mRNAs of 500, 700 and 1400 bases can be detected using oligonucleotide probes specific for the genes sfaB, sfaC and sfaA. SfaB and SfaC arepositive regulators infiuencing fimbriation and the production of the S-specific adhesin which is encoded by the gene sfaS Iocated in the distal half of the determinant. In addition, it is demonstrated that SfaB and SfaC interfere with the regulatory effect of the histone-like protein H-NS, encoded by a locus termed drdX or osmZ. In a drdx+ strain the regulators are necessary for transcription of the sfa determinant. In contrast, sfa expression is activator-independent in a drdx- strain. In this latter genetic background, a substantial fraction of the sfa transcripts is initiated from promoter pA. On the basis of these data we discuss a model for the regulation of this adhesin-specific determinant.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{SchrotenSteinigPlogmannetal.1992,
  author    = {Schroten, H. and Steinig, M. and Plogmann, R. and Hanisch, F. G. and Hacker, J{\"o}rg and Herzig, P. and Wahn, V},
  title     = {S-fimbriae mediated adhesin of Escherichia coli to human buccal epithelial cells is age independent},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59830},
  year      = {1992},
  abstract  = {S-fimbriated Escherichia coli, which cause sepsis and meningitis in the newbom, bind to sialic acid-containing glycoprotein structures on the surface of human buccal epithelial cells. The dependence of · this binding on host age was examined. S-fimbriated · E. coli adhered in comparable numbers to cells in newborns, infants, children and adults (23.0 ± 8.6; 23.1 ± 11.5; 24.7 ± 7.9; 28.9 ± 8.8). Thus, the increased susceptibility of neonates to infections caused by S-fimbriated E. coli cannot be explained by enhanced · adhesion to epithelial cells},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OttBenderLuecketal.1992,
  author    = {Ott, M. and Bender, L. and L{\"u}ck, P. C. and Meyer, P. and Hacker, J{\"o}rg},
  title     = {Distribution of Legionellae in a hospital water system: prevalence of immunologically and genetically related Legionella pneumophila serogroup 6 isolates},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59827},
  year      = {1992},
  abstract  = {A hospital warm water system was monitored for the prcsence and distribution of lcgionellac. Subtyping of ten scletled Legionella pneumophiltl isolates. originating from four different sites in the system by using serogroup spccific antisera in an indircct immunofluorcscence tcst, rcvcalcd that nine of the tcn isolatcs belonged to scrogroup 6, while the remaining one was serogroup I 0. Two monoclonal antibodics (mAbs) spccific for a subgroup of serogroup 6 strains were further used for characterization. None of the strains reactcd with these mAbs. Genome analysis by elaborating Not I profiles using the pulscd field gel electrophoresis (PFGE) technique revealed that nearly all serogroup 6 isolates dcrived from different sites, including a new building connected hy a ring pipe. wcrc identical according to restriction fragment pattems. The patterns were distinguishable from those of the two L. pnewnophi/a serogroup 6 rcfcrencc strains, and ftom that of thc L. pneumophila scrogroup 10 isolate. These data arguc for a relatively homogeneaus L. pneunwpltila serogroup 6 population in the entire watcr system.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{LinhardtZiebuhrMeyeretal.1992,
  author    = {Linhardt, F. and Ziebuhr, W. and Meyer, P. and Witte, W. and Hacker, J{\"o}rg},
  title     = {Pulsed-field gel electrophoresis of genomic restriction fragments as a tool for the epidemiological analysis of Staphylococcus aureus and coagulase-negative Staphylococci},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59811},
  year      = {1992},
  abstract  = {Thirtccn StttJ1hylococcus dw·eus and s: <'pid<'l'· midis strains ohtaincd from nnsc and hand nf twn cmployccs and onc paticnt uf a mcdical ward as weil as two S. hemol.\"licus strains wcrc analyscd according to thcir rcstrktion fmgmcnt lcngth pattcrns ( RFLP) hy pulscd-ficld gcl clcctrophorcsis (PFGE) using thc rcslriction cnzymcs SmaJ and s.. .· tll. Spccics idcntification nf thc isolatcs was pcrformcd hy a systcm which includcs :!O hiochcmical rc"ctions. Furthcrmorc. thc antillintic resistancc pattcrns of thc stmins wcrc dctcrmincd. Whilc scvcral isolatcs cxhihitcd idcnticaf antihiotic susccptihilitics and hiochcmical prnfilcs. diffcrences in thc RFLP wcrc ohtaincd. ln thrcc cascs, S. epiderm{\"u}lis strains colonizing thc skin showcd an idcntical rcstriction profilc as isollltcs from thc mucous mcmhrancs of thc samc pcrson. Wc C(mcludcd that thc analysis of staphylococcal strains hy PFGE is an important cpidcmiolngical tnnl with high discrimination power.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{SchrotenLethenHanischetal.1992,
  author    = {Schroten, H. and Lethen, A. and Hanisch, F., G. and Plogmann, R. and Hacker, J{\"o}rg and Nobis-Bosch, R. and Wahn, V.},
  title     = {Inhibition of adhesion of S-fimbriated Escherichia coli to epithelial cells by meconium feces of breast fed and formula fed newborns - mucins are the major inhibitor component},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59804},
  year      = {1992},
  abstract  = {We investigated the ability of meconium, feces from human milk-fed (HMF) newborns, and feces from formula-fed (FF) newborns to inhibit adhesion of S-fimbriated E. coli to human buccal epithelial cells. S-fimbriae are a common property of E.·coli strains causing sepsis and meningitis in neonates. Meconium had the highest content of neuraminic acid and the strongest inhibitory effect on bacterial adhesion. HMF also exerted high inhibitory activity while FF was markedly less active: To achieve inhibitory effects comparable to HMF a sixfold amount of FF was required. Glycoproteins from excretions were separated by gel chromatography. Fractions obtained were analyzed for adhesion-inhibiting activity. In all excretions analyzed, the mucin-containing fraction could be identified as the major inhibitory component. Inhibition was probably mediated by specific interaction of this fraction with S-fimbriae, as shown by binding of isolated fimbriae on Western blots after electrophoretic separation of glycoproteins. In conclusion, our data support the view that the mucin-containing fraction from meconium and human milk exerts antibacterial functions by preventing adhesin-mediated binding of pathogenic bacteria to mucosal epithelia. Key Words: S-fimbriated E. coli-Inhibition of adhesion-Meconium- Feces of human milk-fed newborns-Feces of formula-fed newborns-Mucins.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{ZinglerOttBlumetal.1992,
  author    = {Zingler, G. and Ott, M. and Blum, G. and Falkenhagen, U. and Naumann, G. and Sokolowska-K{\"o}hler, W. and Hacker, J{\"o}rg},
  title     = {Clonal analysis of Escherichia coli serotype O6 strains from urinary tract infections},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59786},
  year      = {1992},
  abstract  = {A total of 36 Escherichia coli urinary tract isolates (UTI) of serotype 06, with different combinations of capsule ( K) and flagellin ( H) antigens, were analysed according to the outer membrane pattern (OMP), serum resistance properties, mannose-resistant hemagglutination using various types of erythrocytes, and also for the genetic presence and the expression of Pfimbriae. S fimbriae/F1 C fimbriae, Type 1 fimbriae, aerobactin and hemolysin. Twenty selected strains were further analysed by pulsed field gel electrophoresis (PFGE), elaborating genomic profilas by Xba I cleavage and subsequent Southern hybridization to virulence-associated DNA probes. lt could be shown that 06 UTI isolates represent a highly heterogeneaus group of strains according to the occurrence and combination of these traits. Relatedness an the genetic and the phenotypic Ievei was found for some of the strains exhibiting the same 0: K: H: F serotype. DNA Iang-range mapping further indicated some interesting features, according to the copy number and the genomic linkage of virulence genes.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{SchrotenHanischPlogmannetal.1992,
  author    = {Schroten, H. and Hanisch, F. G. and Plogmann, R. and Hacker, J{\"o}rg and Uhlenbruck, G. and Wahn, V.},
  title     = {Inhibition of Adhesion of S-fimbriated Escherichia coli to buccal epithelial cells by human milk fat globule membrane components: a novel aspect of protective function of mucins in the non-immunoglobulin fraction},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59793},
  year      = {1992},
  abstract  = {We investigated the presence of factors in human milkthat inhibit Invasion of pathogenic bacteria. The efl'ect of human milk fat globule membrane (HMFGM) components on adhesion of cloned S-fimbriated Escherichia coli to human buccal epithelial cells was analyzed. S fimbriae are a common feature of E. coli strains causing sepsis and meningitis in newborns and are bound to epithelia via sialyl-(a-2-3)galactoside structures. Human milk fat globules (HMFG) could be agglutinated by the above-mentioned bacteria. Agglutination could be inhibited by fetuin, human glycophorin, and a 1-acid glycoprotein. In addition, pretreatment of HMFG with Jlibrio cholerae neuraminidase markedly reduced bacterium-induced agglutinations, indicating the involvement of neuraminic acid-containing glycoproteins. In contrast, Iipid droplets of infant formula or artificiallipid emulsions (Intralipid) could not be agglutinated. HMFG were present in stools of breast-fed neonates as shown by indirect immunofluorescence staining with a monoclonal antibody directed against carbohydrate residues present on HMFGM. These HMFG could be agglutinated by bacteria. HMFG inhibited E. coli adhesion to buccal epithelial cells. To further characterize relevant E. coli binding structures, HMFGM components w~re separated by gel chromatography. The mucin fraction showed the most pronounced inhibitory efrect on adhesion of S-fimbriated E. coli to human buccal epithelial cells. Our data soggest that HMFG inhibit bacterial adhesion in the entire intestine and thereby may provide protection against bacterial infection.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{FischerBangLudwigetal.1992,
  author    = {Fischer, G. and Bang, H. and Ludwig, B. and Mann, K. H. and Hacker, J{\"o}rg},
  title     = {Mip protein of Legionella pneumophila exhibits peptidyl-prolyl cis-trans-isomerase (PPIase) activity},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59778},
  year      = {1992},
  abstract  = {Legfonells pneumoph/la is an intracellular paraslte which ts able to survtve and multipJy in human monocytes and alveolar macrophages. The Mtp (macrophage lnfectiv1ty potentlator) protein has been shown to be an essential virulente factor. A search of translated nuclelt .acld data ba.ses has shown that the Mip proteJn from strain Wadsworth possesses reglons homologaus to those found in the FK.506-bindfng proteins (FKBPs) of several different eukaryotlc organisms. FKBPs are abte to bind to the fmmunosuppressant macrollde FK506 and possess peptidyf .. prolyl cisltrans Isomerase (PPiase) activlty. The gene coding for the Mlp proteln was cloned from the ehromo. some of L. pneumophila straln Philadelph·a I and sequenced. II was synthesl\%ed in Escherichla coll ·K- 12 and alter purlfication it exhibited PPiase activity catalyslng the slow clsltrans lsomerization of prolyl peptlde bonds. ln ollgopeptides. Mip ls inhibi~ted by FK506 and fully reslstant to cyclosporln A, as was also found for the recently characterlzed FKBP-type PPiases of eukaryotes. However, the N-terminal extenslon of Mip and/or the substltutrons of the vari· ab1e amlno acrds ln the C-termlnal FKBP core Iead to variatlons,. when compared with eukaryotlc FKBPs, Jn substrate specfflclty wlth the Oligopeptide substrates of' type Suc-Aia-Xaa-Pro-Phe·4·nitroanUide. Never· theless, the Legionella Mip factor represents a bacte· rial gene product whtch shares some characteristics normally found in eukaryotic proteins. ln view of the activity of PPiases in protein-folding reactlonsf such prokaryotic FKBP analogues may represent a new class of bacterial. pathogenicity factors.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OttBenderChirinosetal.1991,
  author    = {Ott, M. and Bender, L. and Chirinos, E. and Ehret, W. and Hacker, J{\"o}rg},
  title     = {Phenotype versus genotype of the 19 kd peptido-glycan associated protein of Legionella (PplA) among Legionellae and other gram-negative bacteria},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59768},
  year      = {1991},
  abstract  = {The protein PpiA (19 kD) cloned from a genomic library of Legionella pneumophila, Philadelphia 1, represents a peptido-glycan associated outer membrane protein in recombinant E. coli K-12 and L. pneumophila. lt exhibits distinct sequence homology to Iipoproteins of Haemophilus influenzae and E. coli. A ppiA specific DNA probe generated by PCR was used in Southern hybridizations of chromosomal DNA of Legionella strains and other Gram-negative pathogens. Under conditions of high stringency, hybridization could only be observed in L. pneumophila isolates, but alt other Legionella strains tested displayed hybridization under lower stringency. No signals appeared after hybridization of chromosomal DNA from a variety of other bacteria. Using anti-PpiA monospecific polyclonal antibodies in Western blots, it was demonstrated that PpiA related proteins of nearly the same size are found in all L. pneumophila isolates and in a variety of, but not alt, the Legionella species analysed here.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OttMessnerHeesemannetal.1991,
  author    = {Ott, M. and Messner, P. and Heesemann, J. and Marre, R. and Hacker, J{\"o}rg},
  title     = {Temperature dependent expression of flagella in Legionella},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59755},
  year      = {1991},
  abstract  = {Legionel/a pneumophila, the causative agent of Legionnaires' disease, was analysed by electron microscopy for production of surface structures. Crystalline surface (S-) layers and fimbriae were not detected, but monotrichous flagellation was seen. Polyclonal antibodies specific for the 47 kDa ftagellin subunit of L. pneumophila Philadelphia I were used in Western blots to confirm the presence of flagella subunits in various L. pneumophila strains tested, but the antiserumalso reacted with flagellin subunits of L. micdlulei, L. hackelia (serogroup (SG) l and SG21 and L./ongbetichae (SG2). Flagellation of Legionellae was shown to be temperature regulated. When the growth temperature of virulent and avirulent variants of strain L. pneumophila Philadelphia I was shifted from 30 oc to either 37 or 41 oc, a decrease in the percentage offtagellated bacteria within the populationwas observed.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{BenderOttDebesetal.1991,
  author    = {Bender, L. and Ott, M. and Debes, A. and Rdest, U. and Heesemann, J. and Hacker, J{\"o}rg},
  title     = {Distribution, expression and long range mapping of legiolysin gene (lly) specific DNA sequences in Legionellae},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59744},
  year      = {1991},
  abstract  = {The legiolysin gene (lly) cloned from Legionella pneumophila Philadelphia 1 confers the phenotypes of hemolysis and browning of the culture medium. An internal Uy-specific DNA probe was used in Southern hybridizations for the detection of Uy-specific DNA in the genomes of legioneUae and other gram-negative pathogenic bacteria. Under conditi9ns of high stringency, tlie Uy DNA probe specifically reacted with DNA fragments fr9m L. pneumophi{\"u}z isolates; by reducing stringency, hybridization was also observed for all other Legionella strains tested. No hybridization occurred with DNAs isolated from bact~ria of other genera. The Uy genewas mapped by pulsed-field gel electrophoresis to the respective genomic Notl fragments of Legionelltz isolates. By using antilegiolysin monospecific polyclonal antibodies in Western blots (immunoblots), Lly proteins could be detected only in L. pneumophila isolates.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OttBenderBlumetal.1991,
  author    = {Ott, M. and Bender, L. and Blum, G. and Schmittroth, M. and Achtmann, M. and Tsch{\"a}pe, H. and Hacker, J{\"o}rg},
  title     = {Virulence patterns and long range mapping of extraintestinal Escherichia coli K1, K5 and K100 isolates: Use of pulse field gel electrophoresis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59738},
  year      = {1991},
  abstract  = {A total of 127 extraintestinal Escherichia coli strains of the capsule serotypes Kl, KS, and KlOO from human and animal sources were analyzed for DNA sequences specific for the genes for various adhesins (P fimbriae fpap] and P-related sequences fprs], S fimbriae [s/a)/FlC fimbriae [foc], and type I fimbriae lfim]), aerobactin (aer), and hemolysin (hly). The expression of corresponding virulence factors was also tested. Twenty-four selected strains were analyzed by long-range DNA mapping to evaluate their genetic relationships. DNA sequences for the adhesins were often found in strains not expressing them, while strains with hemolysin and aerobactin genes usually did express them. Different isolates of the same serotype orten expressed different virulence patterns. The use of virulence-associated gene probes for Southern hybridization with genomic DNA fragments separated by pulsed-field gel electrophoresis revealed that a highly heterogeneous restriction fragment length and hybridization pattern existed even within strains of the same serotype. Long-range DNA mapping is therefore useful for the evaluation of genetic relatedness among individual isolates and facilitates the performance of .precise molecular epidemiology.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{LudwigSchmidMarreetal.1991,
  author    = {Ludwig, B. and Schmid, A. and Marre, R. and Hacker, J{\"o}rg},
  title     = {Cloning, genetic analysis and nucleotide sequence of a determinant coding for a 19 kd peptidoglycan-associated protein (Ppl) of Legionella pneumophila},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59721},
  year      = {1991},
  abstract  = {A genomic library of Legionello pneumophihz, the causative agent of Legionnaires disease in humans, was constructed in Escherichill coli K-12, and the recombinant clones were screened by immuno-colony blots with im antiserum raised against heat-killed L. pneumophilo. Twenty-three clones coding for a LegioneUa-specific protein of 19 kDa were isolated. The 19-kDa protein, which represents an outer membrane protein, was found tobe associated with the peptidoglycan layer bothin L. pneumophilo andin the recombinant E. coli clones. This was shown by electrophoresis and Western immunoblot analysis of bacterial cell membrane fractions witb a monospecific polyclonal 19-kDa protein-specific antiserum. Tbe protein was termed peptidoglycan-associated protein of L. pneumophilo (Ppl). The corresponding genetic determinant, ppl, was subcloned on a 1.8-kb Clol fragment. DNA sequence studies revealed that two open reading frames, pplA and pplB, coding for putative proteins of 18~9 and 16.8 kDa, respectively, were located on the Clol fragment. Exonuclease 111 digestion studies confirmed tbat pplA is the gene coding for the peptidoglycan.;.associated 19-kDa protein of L. pneumophilo. The amino acid sequence of PpiA exhibits a high degree of homology to the sequences of the Pal Iipoproteins of E. coli K-12 and liaemophilus injluenvze.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{BlumOttCrossetal.1991,
  author    = {Blum, G. and Ott, M. and Cross, A. and Hacker, J{\"o}rg},
  title     = {Virulence determinants of Escherichia coli O6 extraintestinal isolates analysed by Southern hybridizations and DNA long range mapping techniques},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59717},
  year      = {1991},
  abstract  = {A total of 16 Escherichia coli 06 strains isolated from cases of extraintestinal infections were analysed for the genetic presence and phenotypic expression of fimbrial adhesins ( P, S/FIC, type I), aerobactin and hemolysin. ln addition restriction fragment length polymorphisms (RFLPs) of Xbal-cleaved genomic DNA of seven selected strains, separated by orthogonal field alternation gel electrophoresis {OFAGE) were determined and virulence-associated DNA probes were used for Southern hybridization studies of the Xbal-cleaved genomic DNAs. The virulence characteristics and hybridization patterns obtained differed between the various isolates. ln three isolates hemolysin genes and P fimbrial determinants were located on the same Xbal fragments. Furthermore, multiple copies of FIC determinants (foc) could be detected in two strains. Our data show that the new technique of pulse field electrophoresis tagether with Southern hybridization represents a powerful tool for the genetic analysis of pathogenic bacteria.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{WintermeyerRdestLudwigetal.1991,
  author    = {Wintermeyer, E. and Rdest, U. and Ludwig, B. and Debes, A. and Hacker, J{\"o}rg},
  title     = {Characterization of legiolysin (lly); responsible for hemolytic activity, colour production and fluorescence of Legionella pneumophila},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59706},
  year      = {1991},
  abstract  = {No abstract available},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OttHacker1991,
  author    = {Ott, M. and Hacker, J{\"o}rg},
  title     = {Analysis of the variability of S fimbriae expression in an Escherichia coli pathogen.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59695},
  year      = {1991},
  abstract  = {The uropathogenic Escherichia coli wiJd..:type strain 536 produces S-fimbriae, P-related fimbriae and type I fimbriae. Using immuno-colony dot and ELISA techniques, variants were detected showing an increased degree of S-fimbrial production. It was demonstrated by itrtmunofluorescence microscopy that in noimal (wild-type) and hyperS- fimbriated E. coli populaiions non-fimbriated cells also · exist, and that the percentage of Sfinibrlated and non-fimbriated bacteria was roughly identica1 in either population. Hyper-Sfimbriated variants could be stably maintained. The transition from wild-type to hyper-S-fimbriation, which occurs spontaneously, is markedly higher than vice versa. Southern blot analysis of the S fimbrial adhesin (sfa) determinants of normal and hyper-fimbriated strains revealed no marked difference in the gene structure.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{HackerOttLudwigetal.1991,
  author    = {Hacker, J{\"o}rg and Ott, M. and Ludwig, B. and Rdest, U.},
  title     = {Intracellular survival and expression of virulence determinants of Legionella pneumophila},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59681},
  year      = {1991},
  abstract  = {Legionella pneumophila, the causative agent of Legionnaires' disease is able to live and multiply within macrophages as weil as within protozoan organisms. Legionella strains inhibit phagosome-lysosome fusion and phagosome acidification. By using two different cell culture systems, one derived from human macrophages and the other from human.embryo lung fibro:blastic cells, it is demonstrated that Legionella strains lose their virulence following cultivation in the laboratory. In order to study the mechanisms involved in intracellular survival of Legionella a genomic library of strain Legionella pneumophila Philadelphia I was established in Escherichia coli K-12. By cosmid cloning technique we were able to clone five putative virulence factors, two of which exhibit hemolytic activities and three of which represent membrane-associated proteins of 19, 26 and 60 kilodalton. One of the hemolytic proteins, termed legiolysin, represents a new toxin which specifically lyses human erythrocytes. The other hemolysin exhibits proteolytic properties in addition and is cytolytic for Vero and CHO cells. Further sturlies will be necessary to determine the exact role of the cloned proteins in the pathogenesis of Legionella. Zusammenfassung: Intrazellul{\"a}res {\"U}berleben},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OttBenderMarreetal.1991,
  author    = {Ott, M. and Bender, L. and Marre, R. and Hacker, J{\"o}rg},
  title     = {Pulsed field electrophoresis of genomic restriction fragments for the detection of nosocomial Legionella pneumophila in hospital water supplies},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59672},
  year      = {1991},
  abstract  = {Ten Legionella pneumophUa strains isolated from dift'erent sources were analyzed according to their restriction fragment patterils obtained by cle~vage of gen.omic DNA With Notl and Sftl and separation by pulsed field electrophoresis. Three L. pneumophila isolate~ from a nosocomial outbreak in L{\"u}~k (Germany) and three other L. prreumophilll stralns independently isolated from a water tap located in the care unit where tbe patients were bospitalized 'xhibited identical restricti9n fragment profiles. Therefore, we concluded that these environment81 spee~ens were the source of the Legionnatres dlsease. Anotber two isolates from patients and two strains from the environment, all unrelated to the outJlreak described, sbowed different cleavage patterns.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{SchmollMorschhaeuserOttetal.1990,
  author    = {Schmoll, T. and Morschh{\"a}user, J. and Ott, M. and Ludwig, B. and Van Die, I. and Hacker, J{\"o}rg},
  title     = {Complete genetic organization and functional aspects of the Escherichia coli S fimbrial adhesin determinant: nucleotide sequence of the genes sfaB, C, D, E, F.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59661},
  year      = {1990},
  abstract  = {The S fimbrial adhesin (sfa) determinant of E. co/i comprises nine genes situated on a stretch of 7.9 kilobases (kb) DNA. Here the nucleotide sequence of the genes sfa B and sfaC situated proximal to the main structural gene sfaA is described. Sfa-LacZ fusions show that the two genes are transcribed in opposite directions. The isolation of mutants in the proximal region of the sfa gene cluster, the construction of sfa-phoA gene fusions and subsequent transcomplementation sturlies indicated that the genes sfaB and sfaC play a role in regulation of the sfa determinant. ln addition the nucleotide sequence of the genes sfa D, sfa E and sfa F situated between the genes sfaA and sfaG responsible for S subunit proteins, were determined. lt is suggested that these genes are involved in transport and assembly of fimbrial subunits. Thus the entire genetic organization of the sfa determinant is presented and compared with the gene clusters coding for P fimbriae (pap), F1 C fimbriae (foc) and type I fimbriae ( fim). The evolutionary relationship of fimbrial adhesin determinants is discussed.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{BenderOttMarreetal.1990,
  author    = {Bender, L. and Ott, M. and Marre, R. and Hacker, J{\"o}rg},
  title     = {Genome analysis of Legionella spp. by orthogonal field alternation gel electrophoresis (OFAGE)},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59657},
  year      = {1990},
  abstract  = {Various Legionella isolates from different sources and origins were analysed by orthogonal field alternation gel electrophoresis of Not I cleaved genomic DNA. The genome of L pneumophila Philadelphia I, the original isolate of the epidemics in 1976, exhibits only five Not I fragments. Two virulent derivatives. derived from L pneumophila Philadelphia I. which were obtained by prolonged passage on artificial cuhure media, did not differ from their isogenic virulent strain according the Not I fragment pattern. By summing the lengths of the Notl fragments, the genome size of L. pneumophila Philadelphia I was calculated as approximately 3.9 Mb. Environmental L pneumophila strains exhibited different Not I pattems, as did Legionella strains not belongi'ng to the species pneumophila. The usefulness of DNA long range mapping of Legionella ssp. with Notl for epidemiology and evaluation of their evolutionary rela· tionships is discussed.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MarreKreftHacker1990,
  author    = {Marre, R. and Kreft, B. and Hacker, J{\"o}rg},
  title     = {Genetically engineered S and F1C fimbriae differ in their contribution to adherence of Escherichia coli to cultured renal tubular cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59644},
  year      = {1990},
  abstract  = {Escherichia coU K-12 strains producing S-fimbrial adhesins, FlC fimbriae, and mutagenized fimbriae were tested in a binding assay with a renal tubular cell line. S-fimbrial adhesins and FlC fimbriae mediated bindlog to tubular cells. The SfaA, SfaG, and SfaS subunits of S fimbriae contributed to attachment. Site-specific mutations in the sfaS gene reduced binding. The Inhibitionprofile of FlC fimbriae resembled that of S fimbriae.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{VenturSchefferHackeretal.1990,
  author    = {Ventur, Y. and Scheffer, J. and Hacker, J{\"o}rg and K{\"o}nig, W.},
  title     = {Effects of adhesins from mannose-resistant Escherichia coli on mediator release from human lymphocytes, monocytes and basophils and from polymorphonuclear granulo-cytes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59636},
  year      = {1990},
  abstract  = {We investigated the roJe of Escherichia coU expressing mannose-resistant hemagglutination and adhesins with regard to the induction of leukotrienes from a suspension of human lymphocytes, monocytes, and basophils (LMBs) compared with human polymorphonuclear granulocytes (PMNs). Genetically cloned E. coli strains expressing various types of mannose-resistant hemagglutination (MRH+) were phagocytosed to a higher degree by monocytes than the nonadherent E. coli strain. The various strains dUfered in their capacity to induce a chemiluminescence response, which showed the same pattern for LMBs and PMNs. Stimulation of LMBs with bacteria alone, unlike granulocytes, did not activate the cells for the release of leukotrienes. However, preincubation of LMBs with bacteria decreased subsequent leukotriene formation when the cells were stimulated with calcium ionophore. The inhibitory eft'ect was dependent on the concentration of bacteria used for preincubation as weil as on the preincubation temperature. The various bacterial strains dift'ered in inhibitory potency for mediator release. Preincubation of LMBs with zymosan, opsonized zymosan, the bacterfal peptide FMLP, and peptidoglycan bad no inhibitory eft'ect or even increased subsequent IeukotrieDe formation. Opsonized bacteria were far less inhibitory than nonopsonized bacteria. In contrast to human LMBs, preincubation of human PMNs with mannose-resistant bacteria led to increased leukotriene 84 generation and reduced w-oxidation of leukotriene 84 • Our data soggest that phagocytes (neutrophils, monocytes) respond in a different way for leukotriene formation after Interaction with mannose-resistant E. coli.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{SchmollOttOugedaetal.1990,
  author    = {Schmoll, T. and Ott, M. and Ougeda, B. and Hacker, J{\"o}rg},
  title     = {Use of a wild-type gene fusion to determine the influence of environmental conditions on expression of the S fimbrial adhesin in an Escherichia coli pathogen},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59625},
  year      = {1990},
  abstract  = {S fimbrial adhesins (Sfa) enable pathogenic Escherichia coli strains to bind to sialic acid-containing eucaryotic receptor molecules. In order to determine the inftuence of culture conditions on the expression of the sfa determinant in a wild-type strain, we fused the gene lacZ, coding for the enzyme ß-galactosidase, to the sfaA gene, responsible for the major protein subunit of S fimbriae. By using a plasmid which carries an R6K origin, the sfaA-Iac hybrid construct was site-specifically integrated into the chromosome of the uropathogenic E. coli strain S36WT. The expression of lacZ, which was under the control of the sfa wild-type promoters, was now equivalent to the sfa expression of strain S36WT. With the help of this particular wild-type construct, it was demonstrated that the sfa determinant is better expressed on solid media than in liquid broth. The growth rate bad a strong inftuence on Sfa expression under aerobic but not under anaerobic conditions. Production of Sfa was further regulated by catabolite repression, osmolarity, and temperature.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MorschhaeuserHoschuetzkyJannetal.1990,
  author    = {Morschh{\"a}user, J. and Hosch{\"u}tzky, H. and Jann, K. and Hacker, J{\"o}rg},
  title     = {Functional analysis of the Sialic acid-binding adhesin SfaS of pathogenic Escherichia coli by site-specific mutagenesis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59613},
  year      = {1990},
  abstract  = {The gene coding for the sialic acid-specific adhesin SfaS produced by the S fimbrial adhesin (sfa) determinant of Escherichia coli has been modified by oligonucleotide-directed, site-specific mutagenesis. Lysine 116, arginine 118, and Iysine 122 were replaced by threonine, serine, and threonine, respectively. The mutagenized gene dusters were able to produce S fimbrial adhesin complexes consisting of the S-specific subunit proteins including the adhesin SfaS. The mutant clones were further characterized by hemagglutination and by enzyme-linked immunoassay tests with antifimbria- and anti-adhesin-specific monoclonal antibodies, one of which is able to block S-specific binding (Moch et al., Proc. Natl. Acad. Sei. USA 84:3462-3466, 1987). The lysine-122 mutantclone was indistinguishable from the wild-type clone in these assays. Replacement of Iysine 116 and ai'ginine 118, however, abolished hemagglutination and resulted in clones which showed a weak (Iysine 116) or a negative (arginine 118) reaction with the antiadhesin-specific antibody Al. We therefore suggest that Iysine 116 and arginine 118 have an inßuence on binding of SfaS to the sialic acid residue of the receptor molecule. Substitution of arginine 118 by serine also had a negative efl"ect on the amount of SfaS adhesin proteins isolated from the S fimbrial adhesin complex.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{HackerBenderOttetal.1990,
  author    = {Hacker, J{\"o}rg and Bender, L. and Ott, M. and Wingeder, J. and Lund, B. and Marre, R. and Goebel, W.},
  title     = {Deletions of chromosomal regions coding for fimbriae and hemolysins occur in vivo and in vitro in various extraintestinal Escherichia coli isolates},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59608},
  year      = {1990},
  abstract  = {No abstract available},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{RiegmannKustersVanVeggeletal.1990,
  author    = {Riegmann, N. and Kusters, R. and Van Veggel, H. and Bergmans, H. and Van Bergen en Henegouwen, P. and Hacker, J{\"o}rg and Van Die, I.},
  title     = {F1C fimbriae of an uropathogenic Escherichia coli: Genetic and functional organization of the foc gene cluster and identification of minor subunits},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59597},
  year      = {1990},
  abstract  = {Tbe genetic organization of tbe foc gene duster bas been studied; six genes involved in tbe biogenesis of Fl C fimbriae were identifi.ed.focA encodes tbe major fimbrial subunit, focC encodes a product tbat is indispensable for fimbria formation,focG andjocH encode minor ftmbrial subunits, andfocl encodes a protein wbicb sbows similarities to the subunit protein FocA. Apart from tbe FocA major subunits, purified FlC fimbriae contain at least two minor subunits, FocG and FocH. Minor proteins of similar size were observed in purified S fimbriae. Remarkably, some mutations in tbe foc gene duster result in an altered 6mbrial morpbology, i.e., rigid stubs or long, curly ftmbriae.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{SchmollHoschuetzkyMorschhaeuseretal.1989,
  author    = {Schmoll, T. and Hosch{\"u}tzky, H. and Morschh{\"a}user, J. and Lottspeich, F. and Jann, K. and Hacker, J{\"o}rg},
  title     = {Analysis of genes coding for the Sialic acid-binding adhesin and two other minor fimbrial subunits of the S-fimbrial adhesin determinant of Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59585},
  year      = {1989},
  abstract  = {The S flmbrial adhesln (Sfa) enables Esch richla colito attach to slalfc acld-containing receptor molecules of eukaryotJc cells. As prevlously reported, the genetlc determinant coding for the Sfa of an E. co/1 06 strain was cloned, the gene codlng for the major fimbrfal subunit was ldentlfled and sequenced and th.e S speclflc adhesin was detected. Here we present evidence that ln addltlon to the major subunit proteln SfaA three other minor subunit proteins, SfaG (17 kD), SfaS (14kD) and SfaH (31 kD) can be isolated from the S..speclfic flmbrial adhesln complex. The genes coding for these minor subunits were ldenblied, mutagenlzed separately and sequenced. Using haemagglutlnatton tests. electron-microscopy and quantitative ELISA assays with monoclonal anti-SfaA and anti-SfaS antlbodles the functlons of the minor subunlts were determined. lt was determlned that SfaS ls ldentlcal to the S-specific adhesln; whlch also plays a role ln deterrninatlon of the degree of fimbri· ation ofthe cell. The mlnor subunit SfaH also had some Jnfluence on the Ievei of fimbrlation of the cell. while StaG ls necessary for full expression of S·specific binding. lt was further shown that the amino-terminal proteln sequence of the isolated SfaS profein was identJcal to the proteln sequence calculated from the DNA sequence of the sfaS gene locus.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MarreHackerBraun1989,
  author    = {Marre, R. and Hacker, J{\"o}rg and Braun, V.},
  title     = {The cell-bound hemolysin of Serratia marcescens contributes to uropathogenicity},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59576},
  year      = {1989},
  abstract  = {No abstract available},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{KoenigKoenigSchefferetal.1989,
  author    = {K{\"o}nig, W. and K{\"o}nig, B. and Scheffer, J. and Hacker, J{\"o}rg and Goebel, W.},
  title     = {Role of cloned virulence factors (mannose-resistant hemagglutination, mannose-resistant adhesins) from uropathogenic Escherichia coli strains in release of inflammatory mediators from neutrophils and mast cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59564},
  year      = {1989},
  abstract  = {Genetically cloned E. co/i strains expressing cloned virulence factors were studied with regard to their capability to induce inflammatory mediator release from various target cells. Among the strains were E. co/i strains with mannose-resistant haemagglutination (MRH +) and mannose-resistant adhesins, e.g. E. coli 536/21 pANN 80 I /4, E. coli 536/21 pANN 921 and E. coli 536/21 pANN 801-1. In comparison, E. coli 536/21, E. coli 536/21 pGB 30 int and E. coli Kl2, without and with mannosesensitive haemagglutination (MSH±), and adhesins were studied. The properties of the various strains for human PMN with regard to adherence and phagocytosis, chemiluminescence, 5-lipoxygenase activation of arachidonic acid, leukotriene formation, granular enzyme release and release of histamine from rat mast cells were analysed. It is evident that the various 'biochemical processes of cell activation are dissociated events. The highest chemiluminescence response is obtained with strains expressing MSH+, P-M RH+ or S-M RH+; the presence of S-adhesins suppressed the response. Highest leukotriene formation is obtained with E. coli 536/21 pANN 801-4, while E. coli with MSH was inactive. The concomitant presence of haemolysin secretion enhanced mediator release significantly. Our data suggest a potent role for mannose-resistant haemagglutination (MRH), adhesins and haemolysin as virulence factors in inducing the release of inflammatory mediators.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MarreHackerWoodetal.1989,
  author    = {Marre, R. and Hacker, J{\"o}rg and Wood, G. and Schmidt, G.},
  title     = {Oral vaccination of rats with live avirulent Salmonella derivatives expressing adhesive fimbrial agents of uropathogenic Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59559},
  year      = {1989},
  abstract  = {The avirulent Salmonella typhimurium F885 was transformed with a plasmid carrying the cloned S fimbriae genes of a uropathogenic Escherichia coli. The resulting transformant (F885-1) produced efficiently E. coli S fimbriae and was used for live oral vaccination of rats. For comparison rats were immunized subcutaneously with isolated S fimbriae. Both routes of vaccination resulted in a significant lgG antibody response to S fimbriae. In addition live oral vaccination induced a serum lgA response against S fimbriae. After transurethral infection of rats with a S fimbriae producing E. coli a 10-fold reduction of bacterial counts in the kidney was observed in rats orally vaccinated with F885-1 as compared to unvaccinated controls. This study suggests that the avirulent Salmonella F885 may be used as a fimbrial antigen carrier for oral vaccination against renal infections.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{KrallmannWenzelOttHackeretal.1989,
  author    = {Krallmann-Wenzel, U. and Ott, M. and Hacker, J{\"o}rg and Schmidt, G},
  title     = {Chromosomal mapping of genes encoding mannose-sensitive (type I) and mannose-resistant F8(P) fimbriae of Escherichia coli O18:K5:H5},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59545},
  year      = {1989},
  abstract  = {DNA hybridization experiments demonstrated that the gene clusters encoding the F8 fimbriae (fei) as well as the type I fimbriae (pi/) exist in a single copy on the chromosome of E. coli 018:K5 strain 2980. In conjugation experiments with appropriate donors, the chromosomal site of these gene clusters was determined. The pil genes were mapped close to the gene clusters thr and Jeu controlling the biosynthesis of threonine and leucine, respectively. The fei genes were found to be located close to the galactose operon (gal) between the position 17 and 21 of the E. coli chromosomallinkage map.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MunoaHackerJuarez1988,
  author    = {Munoa, F. and Hacker, J{\"o}rg and Juarez, A.},
  title     = {Characterization of a chromosomal mutant that blocks hemolysin excretion in Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59534},
  year      = {1988},
  abstract  = {We analyzed an Escherichia coli strain which harbours a chromosomal mutation that blocks the hemolysin excretion. Compartmentation studies showed that hemolysin accumulates in the cytoplasm and not in the periplasm. The mutation did not affect the SDS-PAGE protein pattern of the outer membrane, although some alterations were apparent in the periplasmic protein pattern. The mutant strain, E. coli Hsb-1 also failed to export a cloned fimbrial adhesin. The mutation maps in the min. 3.5 of the E. coli genetic map.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{PawelzikHeesemannHackeretal.1988,
  author    = {Pawelzik, M. and Heesemann, J. and Hacker, J{\"o}rg and Opferkuch, W.},
  title     = {Cloning and characterization of a new type of fimbria (S/F1C-related fimbria) expressed by an Escherichia coli O75:K1:H7 blood culture isolate},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59529},
  year      = {1988},
  abstract  = {The Escherichia coli blood culture isolate BK658 (07S:K1:H7) expresses F1A and F1B fimbriae as weil as a third fimbrial type which reacts with anti-S-fimbrial antiserum but fails to show S-specific binding properlies (i.e., agglutination of bovine erythrocytes). To characterize these fimbriae, we cloned the respective genetic determinant in E. coli K-12. The resulting recombinant clone HB101(pMMP658-6) expresses fimbriae of 1.2-p.m length and a diameter of approximately 7 nm. The determinant codes for the fimbrillin subunit, a protein of 17 kUodaltons in size, and for at least five other proteins of 87, 31, 23, 14.3, and 13.8 kUodaltons. By restriction analysis and by DNA-DNA hybridization, it could be shown that the cloned fimbrial determinant of strain BK658 exhibits a high degree of sequence homology to the gene clusters coding for S fimbrial adhesins (sfa) and F1C fimbriae (/oc). By using the Western blot (immunoblot) technique and a quantitative enzyme-linked immunosorbent assay, it could be further demonstrated that the cloned fimbriae of BK658, S fimbriae, and FlC fimbriae share cross-reactive epitopes as weil as antigenic determinants specific for each fimbrial type. No antigenic cross-reactivity with F1C fimbriae could be detected. The results indicate a genetical and serological relatedness of the cloned fimbriae toS fimbriae and F1C fimbriae. Therefore, this new type of fimbriae is preliminarily termed SIF1C-related fimbriae (Sfr).},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OttHoschuetzkyJannetal.1988,
  author    = {Ott, M. and Hosch{\"u}tzky, H. and Jann, K. and Van Die, I. and Hacker, J{\"o}rg},
  title     = {Gene clusters for S fimbrial adhesin (sfa) and F1C Fimbriae (foc) of Escherichia coli: Comparative aspects of structure and function},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59519},
  year      = {1988},
  abstract  = {Fimbrial 8dhesins en8ble b8cteria to 8ttach t9 eucaryotic ceU~. The genetic determin8nts for S fimbrial 8dhesins (sja) an.d for FlC ("pseudotype I") fimbri8e ifoc) were compared. Sfa and FlC represent functionally distinct 8dbesins in tbeir receptor specificities. Nevertheless, 8 high degree of bomology between both determin8nts was found on the basis of DNA-DNA hybridizations. Characteristic difl'erences in the restriCtion maps of tbe corresponding gene clusters, bowever, were visible in regions coding for the fimbrial subunits and for the S-specific 8dhesin. While a plasmid carrying the geneiic deternlinant for FlC fimbri8e was 8ble to complement transposon-induced sfa mutants, 8 plasmid carrying tbe genetic determin8nt for 8 tbird 8dht\$in type, termed P fimbriae, was un8ble to do so. Proximal sfa-specific sequences carrying the S fimbrial st'"uctural gene were fused to sequences representing tbe di\$tal part of the foc gene cluster to form 8 hybrid cluster, and tbe foc proxim~ region coding for tbe structural protein was Iigated to sfa distal sequences to form 8 second hybrid. Botb hybrid clones produced intact fimbriae. Anti-FlC monoclonal8ntibodies (MAbs) only recognized clones which produced FlC fimbriae, and an ~ti-S 8dhesin MAb marked clones whicb expressed the S adhesin. Bowever, one of four other anti-S fimbri8e-specific MAbs reacted witb both fimbrial structures, S and FlC, indicating 8 common epitope on both antigens. The results presented bere ~upport tbe view th8t sfa and foc determinants code for fimbri8e tb8t 8re simil8r in several aspects, wbile the P fimbri8e are members of 8 more distantly rel8ted group.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{ParkkinenKorhonenPereetal.1988,
  author    = {Parkkinen, J. and Korhonen, T. K. and Pere, A. and Hacker, J{\"o}rg and Soinila, S.},
  title     = {Binding sites in the rat brain for Escherichia coli S fimbriae associated with neontal meningitis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59500},
  year      = {1988},
  abstract  = {Escherichia coli strains that cause sepsis and meningitis in neonatal infants carry S fimbriae that bind to sialyl galactoside units of cell surface glycoproteins. To investigate the possible role of S fimbriae in determining the tissue tropism of neonatal menlngitis, we have studied the preselice of binding sites for S fimbriae in different tissues of the neonatal rat which is susceptible to meningitis caused by S-fimbriated E. coli. Purified S fimbriae were incubated on cryostat sections of different rat oipns and their bindina was assessed by indirect immunofluorescence. In the bnin of the neonatal rat, S fimbriae specifically bound to the luminal surfaces of the vascular endothelium and of the epithelium lining the choroid plexuses and bnin ventricles. The · bindlog W.s completely inhibited by the trisaccharide NeuAca2-3Ga)ßl-4Gic, a receptor analogue of S fimbriae, and by a preceding neuraminidase treatment of the sections. A recombinant E. coli strain expressina S fimbriae adhered in large numbers to the same tissue sites in the neonatal brain sections as did the purified fimbriae, · whereas the nonfimbriated host strahi and a recombiiuuit strain expresslog P fi.mbriae did not adhere to brain tissues. The results soggest that adhesion of S-fimbriated bacteria to the binding sites observed in the neonatai bnin has a pathogenetic roJe durlog bacterial Invasion from cii'culation into the cerebrospinal fluid.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OttSchmollGoebeletal.1987,
  author    = {Ott, M. and Schmoll, T. and Goebel, W. and Van Die, I. and Hacker, J{\"o}rg},
  title     = {Comparison of the genetic determinant coding for the S-fimbrial adhesin (sfa) of Escherichia coli to other chromosomally encoded fimbrial determinants},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59499},
  year      = {1987},
  abstract  = {DNA probes specific for different regions of the S-fimbrial adhesin (sja) determinant were constructed and hybridized with DNA sequences coding for P (F8 and F13), mannose-sensitive hemagglutinating type 1 (FlA), and FlC fimbriae. While the sfa and F1C DNA determinants exhibited homology along their entire lengths, the P-fimbrial and type 1-fimbrial determinants exhibited homology to regions of the sfa duster responsible for the control of transcription and, to a minor extent, to regions coding for proteins involved in biogenesis and/or adhesion of the fimbriae and for the N-terminal part of the fimbrillin subunit.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{SchmollHackerGoebel1987,
  author    = {Schmoll, T. and Hacker, J{\"o}rg and Goebel, W.},
  title     = {Nucleotide sequence of the sfaA gene coding for the S fimbrial protein subunit of Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59480},
  year      = {1987},
  abstract  = {The sfaA gene of the uropathogenic Escherichia coli 06 strain 536, which is responsible for the determination of the S fimbrial protein subunit, was sequenced. The structural gene codes for a polypeptide of 180 amino acids including a 24-residue N-terminal signal sequence. A size of 15.95 kDa was calculated for the processed SfaA protein. The nucleotide and deduced amino acid sequences show significant homology to those of the F1C fimbria and, to a lesser extent, of the mannose- sensitive hemagglutinating fimbria (FimA, PilA). Only week homology toP fimbriae subunits (F72 , Pap) was found.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MarreHacker1987,
  author    = {Marre, R. and Hacker, J{\"o}rg},
  title     = {Role of S and common type I-fimbriae of Escherichia coli in experimental upper and lower urinary tract infection},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59468},
  year      = {1987},
  abstract  = {No abstract available},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{KoenigKoenigSchefferetal.1986,
  author    = {K{\"o}nig, B. and K{\"o}nig, W. and Scheffer, J. and Hacker, J{\"o}rg and Goebel, W},
  title     = {Role of Escherichia coli α-hemolysin and bacterial adherence infection - requirement for release of inflammatory mediators from granulocytes and mast cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59451},
  year      = {1986},
  abstract  = {We investigated the role of bacterial mannose-resistant fimbriation of S fimbriae (Firn), mannose-resistant hemagglutination (S-Mrh), and hemolysin (Hiy) production by an Escherichitl coli parent and genetically cloned strains as regards (i) their eß'ect on histamine release from rat mast ceUs and (ii) generation of the chemiluminescence response, leukotriene, and enzyme release from human polymorphonuclear granulocytes. These mediators are involved in the induction of inftammatory disease processes and Iead, e.g., to the enhancement of vascular permeability, chemotaxis, aggregation of granulocytes (leukotriene 8 4), lysosomal enzyme release, and smooth-muscle contraction (leukotrienes C4, D4, and E4). The content of azurophilic and specific granules in polymorphonuclear granulocytes consists of highly reactive enzymes which amplify inflammatory reactions. Washed bacteria (E. coli 764 my:t:, E. coli 21085 Hly:t:, E. coli 536 Hly:t: Firn:~: Mrh:t:), as weil as their culture supernatants, were analyzed at various times during their growth cycle. No differences exist between parent and cloned or mutant strains with respect to their outer . membrane proteins and lipopolysaccharide pattern. Washed bacteria [E. coli 764 and 21085(pANN202-312)] which produced hemolysin, unlike my- strains, induced high Ievels of histamine release from rat mast ceUs and led to a significant chemiluminescence response and enzyme and leukotriene release from human polymorphonuclear granulocytes. Bacterial culture supernatants from Hly+ and secreting strains showed similar results with the exception of E. coli 21085(pANN202-312), which is a hemolysin-producing bot not a secretory strain. Our data soggest a potent role for hernolysin as a stimulus for noncytotoxic mediator release from various cells. Furthermore, we showed that the presence of Firn and S Mrh potentiales mediator release. The simultaneous presence of Mrh and Firn [E. coli 535/2l(pANN801-4)] increased mediator release compared with Mrh+ Firn- strains [E. coli 536/21(pANN801-1)]. E. coli 536/21 (Msh- Mrh- Firn- Hly-) did not induce mediator release. Escherichia coli alpha-hemolysin is a protein that causes in vitro Iysis of erythrocytes from several species of animals (6, 12, 1~18, 23). Hemolysin-producing E. coli strains occur only infrequently in the normal fecal ftora of humans but are often isolated from patients with extraintestinal infections such as urinary tract infections, bacteremia, and septicemia (13, 22, 25, 36-38, 46-48). The high percentage of Hly+ E. coli strains among isolates from patients with urinary tract infections suggested that hemolysin contributes to the virulence of E. coli strains. The role of hemolysin as a virulence factor has been recently demonstrated by using various animal models and cell cultures. Alpha-hemolysin is one of the very few proteins produced by members of the family Enterobacteriaceae that is released extracellulary. The genetic control of alpha-hemolysin production, transport, and release from cells is complex (24, 26, 30). At least four genes located on the bacterial chromosome or on ]arge transmissible plasmids are required to elicit a cell-free hemolytic phenotype. Bobach and Snyder (6) suggested that the existence of alpha-hemolysin complexed with lipopolysaccharide may have important implications in the understanding of its biological effects. In addition to hemolysin production, a variety of factors, e.g., fimbriae, expression of specific hemagglutination, and • Corresponding author. 886 0 and K antigens, may contribute to the vi},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MarreHackerHenkeletal.1986,
  author    = {Marre, R. and Hacker, J{\"o}rg and Henkel, W. and Goebel, W.},
  title     = {Contribution of cloned virulence factors from uropathogenic E. coli strains to nephropathogenicity in an experimental rat pyelonephritis model},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59445},
  year      = {1986},
  abstract  = {Escherichia coli 536 (06:K15:H31), which was isolated from a case of urinary tract infection, determines high nephropathogenicity in a rat pyelonephritis system as measured by renal bacterial counts 7 days after infection. The loss of S fimbrial adhesin formation (Sfa-) (mannose-resistant hemagglutination [Mrh-] and fimbria production [Fim-]), serum resistance (Sre-), and hemolysin production (Hly-) in the mutaßt 536-21 led to a dramatic reduction of bacterial counts from almost tOS to only 40 cells per g of kidney. The reintroduction of the cloned S fimbrial adhesin determinant (sfa) increases the virulence of the avirulent mutant strain by a factor of 20; almost the same eß'ect was observed after restoration of serum resistance by Integration of an sja+ recombinant cosmid into the chromosome. Additional reintroduction of the my+ phenotype by Iransformation of two hly determinants increased the virulence of the strains. Demolysin production determined increased renal elimination of leukocytes and erythrocytes. Thus all three determinants investigated, S fimbriae, serum resistance, and hemolysin, contribute to the multifactorial phenomenon of E. coli nephropathogenicity.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OttHackerSchmolletal.1986,
  author    = {Ott, M. and Hacker, J{\"o}rg and Schmoll, T. and Jarchau, T. and Korhonen, T. K. and Goebel, W},
  title     = {Analysis of the genetic determinants coding for the S fimbrial adhesin (sfa) in different Escherichia coli strains causing meningitis or urinary tract infections},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59432},
  year      = {1986},
  abstract  = {Recently we have described the molecular cloning of the genetic determinant coding for the S-fimbrial adhesin (Sfa), a sialic acid-recognizing pilus frequently found among extraintestinal Eschenchili coli isolates. Fimbriae from the resulting Sfa + E. coli K-12 clone were isolated, and an Sfa-specific antiserum was prepared. Western blots indicate that S fimbriae isolated from different uropathogenic and meningitis-associated E. coli strains, including 083:Kl isolates, were serologically related. The Sfa-specific antibodies did not cross-react with P fimbriae, but did cross-react with FlC fimbriae. Furthermore the sja+ recombinant DNAs and some cloned s/a-flanking regions were used as probes in Southem experiments. Chromosomal DNAs isolated from 018:Kl and 083:Kl meningitis strains with and without S fimbriae and from uropathogenic 06:K + strains were hybridized against these sfa-specific probes. Only one copy of the sfa determinant was identified on the chromosome of these strains. No sfa-specific sequences were observed on the chromosome of E. coli K-12 strains and an 07:Kl isolate. With the exception of small alterations in the sfa-coding region the genetic determinants for S fimbriae were identical in uropathogenic 06:K + and meningitis 018:Kl and 083:Kl strains. The sfa determinant was also detected on the chromosome of Kl isolates with an Sfa-negative phenotype, and specific cross-hybridization signals were visible after blotting against FlC-specific DNA. In addition homology among the different strains was observed in the sfa-flanking regions.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{HackerHofEmoedyetal.1986,
  author    = {Hacker, J{\"o}rg and Hof, H. and Em{\"o}dy, L. and Goebel, W.},
  title     = {Influence of cloned Escherichia coli hemolysin genes, S fimbriae and serum resistance on pathogenicity in different animal models},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59423},
  year      = {1986},
  abstract  = {The virulence of the uropathogenic E. coli strain 536 (06: K 1 5: H31) which produces the S-fimbrial adhesin (Sfa•), is serum-resistant (Sre+) and hemolytic (Hiy+) and its derivatives were assessed in five different animal models. Cloned hemolysin (h/y) determinants from the Chromosomes of 06,018 and 075 E. colistrains and from the plasmid pHiy152 were introduced into the spontaneaus Sfa-, Sre-, Hly- mutant 536-21 and its Sfa+, Sre+, Hly- variant 536-31. As already demonstrated for the 536-21 strains {lnfect. Immun. 42: 57-63) the 018-hly determinant but not the plasmid-encoded hly determinant of pHiy 1 52 transformed into 536-31 contribute to lethality in a mouse peritonitis modal. Similar results were obtained with both Hlyhost strains and their Hly+ transformants in a chicken embryo test and in a mouse nephropathogenicity assay in which the renal bacterial counts were measured 1 5 min to 8 hours after i.v. infection. S-fimbriae and serum resistance had only a marginal influence in these three in vivo systems. ln centrast all three factors, S-fimbriae, serum resistance and hemolysin, were necessary for full virulence in a respiratory mouse infection assay. ln a subcutaneously-induced sepsis model in the mouse restoration of S-fimbriae and serum resistance and separately chromosomally-encoded hemolysis increased virulence to a Ievel comparable to that of the parental 536 strain.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{KorhonenParkkinenHackeretal.1986,
  author    = {Korhonen, T. K. and Parkkinen, J. and Hacker, J{\"o}rg and Finne, J. and Pere, A. and Rhen, M. and Holth{\"o}fer, H},
  title     = {Binding of Escherichia coli S fimbriae to human kidney epithelium},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59415},
  year      = {1986},
  abstract  = {Purified S fimbriae and an Escherichia coli strain carrying the recombinant plasmid pANN801-4 that encodes S fimbriae were tested for adhesion to frozen sections of human kidney. The fimbrlae and the bacteria bound to the same tissue domains, and in both cases the binding was specifically inhibited by the receptor analog of S fimbria, sialyl(a2-3)1actose. S fimbriae bound specifically to the epithelial elements in the kidneys; to the epithelial cells of proximal and distal tubules as weil as of the collecting ducts and to the visceral and parietal glomerular epithelium. In addition, they bound to the vascular endothelium of glomerull and of the renal Interstitium. No blnding to connective tissue elements was observed. The results suggest that the biological functlon of S fimbriae is to mediate the adheslon of E. coli to human epithelial and vascular endothellal ceUs.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{KnappHackerJarchauetal.1986,
  author    = {Knapp, S. and Hacker, J{\"o}rg and Jarchau, T. and Goebel, W},
  title     = {Large, Unstable Inserts in the Chromosome Affect Virulence Properties Of Uropathogenic Escherichia coli 06 Strain 536},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59402},
  year      = {1986},
  abstract  = {The hemolytic, uropathogenic Escherichia coli 536 (06:K15:H31) contains two inserts in its chromosome (insert I and insert II), both of which carried hly genes, were rather unstable, and were deleted spontaneously with a frequen~y of 10-3 to 10-4• These inserts were not found in the chromosome of two nonhemolytic E. coli strains, whereas the chromosomal ~equences adjacent to these inserts appeared tobe again homologous in the uropathogenic and two other E. co{\"u} strains. Insert I was 75 kilobases in size and was ftanked at both ends by 16 base pairs (bp) (TTCGACTCCTGTGATC) which were arranged in direct orientation. For insert I it was demonstrated that deletion occurred by recombination between the two 16-bp ftanking sequences, since mutants lacking this insert still carried a single copy of the 16-bp sequence in the chromosome. 8oth inserts contained a functional hemolysin determinant. However, the loss of the inserts not only atfected the hemolytic phenotype bot led to a considerable reduction in serum resistance and the loss of mannose-resistant hemagglutination, caused by the presence of S-type funbriae (sja). lt is shown that the Sfa-negative phenotype is due to a block in transcription of the sfa genes. Mutants of strain 536 which lacked both inserts were entirely avirulent when tested in several animal model systems.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{HackerOttSchmidtetal.1986,
  author    = {Hacker, J{\"o}rg and Ott, M. and Schmidt, G. and Hull, R. and Goebel, W.},
  title     = {Molecular cloning of the F8 fimbrial antigen from Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59391},
  year      = {1986},
  abstract  = {The genetic determinant coding for the Pspecific F8 fimbriae was cloned from · the chromosome of the Escherichia coli wild-type strain 2980 (018: K5: H5: FlC, F8). The F8 determinant was further subcloned into the Pstl site of pBR322 and a restriction map was established. In a Southern hybridization experiment identity between the chromosomally encoded F8 determinant of 2980 and its cloned Counterpart was demonstrated. The cloned F8 fimbri{\"a}e and those of the wild type strain consist of a protein subunit of nearly 20 kDa. F8 fimbriated strains were agglutinated by an F8 polyclonal antiserum, caused mannose-resistant hemagglutination and attached to human uroepi thellal cells. The cloned F8 determinant was weil expressed in a variety of host strains.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MoserOrskovHackeretal.1986,
  author    = {Moser, I. and Orskov, I. and Hacker, J{\"o}rg and Jann, K.},
  title     = {Characterization of a monoclonal antibody against the fimbrial F8 antigen of Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59385},
  year      = {1986},
  abstract  = {A monoclonal lgG 1 antibody against F8 fimbriae was obtained with the hybridoma technique using spieen cells from C3H/f rnice immunised with a fimbrial preparation of Escherichia coli 2980 (018ac: K5: H-: FIC, F8) and Sp 2/0 Ag8 myeloma cells. The hybrid cells were cloned twice by lirniting dilution and grown in tissue culture. The monoclonal antibody was purified from culture supernatants on Protein A Sepharose. lt reacted with F8 fimbriae in colony blot, enzyme-linked immunosorbent assay (ELISA) and immunoblot after electrotransfer from sodium dodecyl sulphate-polyacrylarnide gel electrophoresis (SOS-PAGE) of fimbrial preparations. The antibody bound to and agglutinated F8-fimbriated bacteria.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{KnappThenWelsetal.1985,
  author    = {Knapp, S. and Then, I. and Wels, W. and Michel, W. and Tsch{\"a}pe, H. and Hacker, J{\"o}rg and Goebel, W},
  title     = {Analysis of the flanking regions from different hemolysin determinants of Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59374},
  year      = {1985},
  abstract  = {The haemolysin (hly) determinant of the plasmid pHly152 contains an IS2 element at 469 bp upstream of the hlyC gene. The sequence at the other (right-hand) end (RS) also shows multiple hybridization with the plasmid pHly152 and the chromosome of some Escherichia coli strains but the nucleotide sequence of this region does not reveal the typical properties of an IS element. Similar arrangements in the regions flanking the hly determinant are also found on various Hly plasmids from uropathogenic E. coli strains. Chromosomal hly determinants Iack both flanking sequences (IS2 and RS) in the immediate vicinity of the hly genes. The sequences immediately upstream of the hlyC gene have been determined from several chromosomal hly determinants and compared with the corresponding sequence of the hly determinant of the plasmid pHly152. We show that these sequences, which contain one promoter (left promoter, phlyL) in all hly determinants tested, vary considerably although common sequence elements can still be identified. In contrast, only relatively few nucleotide exchanges have been detected in the adjacent structural hlyC genes. The A + T content of the 200 bp sequence upstream of hlyC is very high (72 mol\% A + T) but even the structural hly genes show a considerably higher A + T content (about 60 mol\%) than the E. coli chromosome on average (50 mol\% A+T) suggesting that the hly determinant may not have originated in E. coli.},
  subject      = {Infektionsbiologie},
  language  = {en}
}