@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{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{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{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{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{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{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{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{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{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{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{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{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{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{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{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{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{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{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{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} }