@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{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{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{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{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{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{HofChristenHacker1986,
  author    = {Hof, H. and Christen, A. and Hacker, J{\"o}rg},
  title     = {Comparative therapeutic activities of Ciprofloxacin, Amoxicillin, Ceftriaxone and Cotrimoxazole in a new model of experimental infection with Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40313},
  year      = {1986},
  abstract  = {A new mouse model for systemic infection with Escherichia coli is presented. Whereas in other models 107_108 bacteria have to be injected into an animal to induce toxic effects resulting in death within 24 hours, now, only 103_104 bacteria of an appropriate strain are required to produce a genuine infection characterized by an increase in the bacterial load over several days. The quantitative determination of bacterial counts per liver allows a more sensitive measurement than recording death rates. Furthermore, few animals are required for a definite result in contrast to the LDso determination of other models. The salient point regarding this new model is that conditioning of animals has to be achieved by incorporating the inoculum into agar which is injected subcutaneously. The resulting infection is completely dependent on the E. colicondistrain used. Whereas a hemolytic, uropathogenic strain is so virulent that an overwhelming infection develops within 48 hours after the injection of 103 bacterial cells, a non-hemolytic variant of this strain is completely avirulent, being unable to multiply in spite of the potentiating agar. The hemolytic E. coli strain ATCC 25922 is intermediate in virulence. The bacterial counts per liver increase steadily until death occurs five to seven days after the injection of 104 bacteria. This bacterial infection can be therapeutically influenced by daily treatment with various drugs. Ciprofloxacin, ceftriaxone and co-trimoxazole are able to cure the infection, whereas amoxicillin given orally is only moderately active against this ATCC strain, which is relatively resistant to amoxicillin.},
  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{BergerHackerJuarezetal.1982,
  author    = {Berger, Harald and Hacker, J{\"o}rg and Juarez, Antonio and Hughes, Colin and Goebel, Werner},
  title     = {Cloning of the chromosomal determinants encoding hemolysin production and mannose-resistant hemagglutination in Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40255},
  year      = {1982},
  abstract  = {We have cloned the chromosomal hemolysin determinants from Escherichia coli strains belonging to the four O-serotypes 04, 06, 018, and 075, The hemolysin-producing clones were isolated from gene banks of these strains which were constructed by inserting partial Sau3A fragments of chromosomal DNA into the cosmid pJC74. The hemolytic cosmid clones were relatively stable. The inserts were further sub cloned either as Sail fragments in pACYC184 or as BamHI-SaLI fragments in a recombinant plasmid (pANN202) containing cistron C (hlye) of the plasmid-encoded hemolysin determinant. Detailed restriction maps of each of these determinants were constructed, and it was found that, despite sharing overall homology, the determinants exhibited minor specific differences in their structure, These appeared to be restricted to cistron A (hlyA), which is the structural gene for hemolysin. In the gene banks of two of these hemolytic strains, we could also identify clones which carried the genetic determinants for the mannose-resistant hemagglutination antigens Vb and VIc. Both of these fimbrial antigens were expressed in the E. coli K-12 clones to an extent similar to that observed in the wild-type strains. These recombinant cosmids were rather unstable, and, in the absence of selection, segregated at a high frequency.},
  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}
}