@article{HughesMuellerHackeretal.1982,
  author    = {Hughes, Colin and M{\"u}ller, Dorothee and Hacker, J{\"o}rg and Goebel, Werner},
  title     = {Genetics and pathogenic role of Escherichia coli hemolysin},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40082},
  year      = {1982},
  abstract  = {While clear evidence exists for the direct involvement of cytolysins in the pathogenesis of Gram-positive bacteria, the significance of Gram-negative haemolysins remains unclear. This paper presents briefly data indicating a role for haemolysin production in infections caused by Escherichia coli and also experiments which have allowed an analysis of the molecular basis of the haemolysis among pathogenic and non-pathogenic strains of this species.},
  language  = {en}
}
@article{HofEmmerlingHackeretal.1982,
  author    = {Hof, H. and Emmerling, P. and Hacker, J{\"o}rg and Hughes, C.},
  title     = {The role of macrophages in primary and secondary infection of mice with Salmonella typhimurium},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40248},
  year      = {1982},
  abstract  = {Elimination of macrophages with high-molecular dextran sulphate (OS) markedly impairs resistance of mice to primary infection with smooth, virulent strains of Salmonella typhimurium, whereas stimulation of this system by killed Bordetella pertussis organisms increases resistance. In infection with rough, avirulent strains of S. iyphimurium the elimination of macro phages was not followed by an essential loss of resistance, and it appears that other non-specific defence mechanisms, for example the complement system, may have compensated for the lack of macrophages. Macrophages, therefore, play an important role in defence during primary infection with virulent strains. In immunity to challenge infection with S. typhimurium, macrophages play an even more significant role. Treatment with OS completely removes immunity, and both humoral and cell-mediated immune mechanisms seem to require the participation of macrophages.},
  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{HackerKnappGoebel1983,
  author    = {Hacker, J{\"o}rg and Knapp, S. and Goebel, W.},
  title     = {Spontaneous deletions and flanking regions of the chromosomal inherited hemolysin determinant of an Escherichia coli 06 strain},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40260},
  year      = {1983},
  abstract  = {The hemolytic Escherichia coli strain 536 (06) propagates spontaneous hemolysin- negative mutants at relatively high rates (10-3 to 10-4 ). One type of mutant (type I) lacks both secreted (external) and periplasmic (internal) hemolysin activity (HlYex - IHlYin -) and in addition shows no mannose-resistant hemagglutination (Mrh -), whereas the other type (type II) is HlYex -IHIYin + and Mrh +. The genetic determinants for hemolysin production (hly) and for mannose-resistant hemagglutination (mrh) of this strain are located on the chromosome. Hybridization experiments with DNA probes specific for various parts of the hly determinant reveal that mutants of type I have lost the total hly determinant, whereas those of type 11 lack only part of the hlyB that is essential for transport of hemolysin across the outer membrane. Using a probe that contains the end sequence of the plasmid pHly152-encoded hly determinant (adjacent to hlyB), we determined that a related sequence flanks also the hlyB-distal end of the chromosomal hly determinant of E. coli 536. In addition several other similar or even identical sequences are found in the vicinity of the hlyC- and the hlyB-distal ends of both the chromosomal and the plasmid hly determinants.},
  language  = {en}
}
@article{KnappHackerThenetal.1984,
  author    = {Knapp, Stefan and Hacker, J{\"o}rg and Then, Irene and M{\"u}ller, Dorothee and Goebel, Werner},
  title     = {Multiple copies of hemolysin genes and associated sequences in the chromosome of uropathogenic Escherichia coli strains},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40278},
  year      = {1984},
  abstract  = {The 06 serogroup Escherichia coli strain 536 carries two hemolysin (hly) determinants integrated into the chromosome. The two hly determinants are not completely identical, either functionally or structurally, as demonstrated by spontaneous deletion mutants carrying only one of them and by cloning each of the two determinants separately into cosmid vectors. Each hly determinant is independently deleted at a frequency of 10-4 , leading to variants which exhibit similar levels of internal hemolysin but different amounts of secreted hemolysin. The two hly determinants were also identified in the 04 E. coli strain 519. The three E. coli strains 251, 764, and 768, which belong to the serogroup 018, and the 04 strain 367 harbor a single chromosomal hly determinant, as demonstrated by hybridization with hly-gene-specific probes. However, a hybridization probe derived from a sequence adjacent to the hlyC-proximal end of the plasmid pHlyl52-encoded hly determinant hybridizes with several additional chromosomal bands in hemolytic 018 and 06 E. coli strains and even in E. coli K-12. The size ofthe probe causing the multiple hybridization suggests a 1,500- to 1,800-base pair sequence directly flanking hlyC. Spontaneous hemolysin-negative mutants were isolated from strains 764 and 768, which had lost the entire hly determinant but retained all copies of the hlyC-associated sequence. This sequence is not identical to a previously identified (J. Hacker, S. Knapp, and W. Goebel, J. Bacteriol. 154:1145-1154, 1983) somewhat smaller (about 850 base pairs) sequence flanking the other (hlyBb-proximal) end of the plasmid pHlyl52-encoded hly determinant which, as shown here, exists also in multiple copies in these hemolytic E. coli strains and in at least two copies in E. coli K-12. In contrast to the plasmid-encoded hly determinant which is directly flanked at both ends by these two diJJerent sequences, the chromosomal hly determinants are not immediately flanked by such sequences.},
  language  = {en}
}
@article{KoenigSchefferBremmetal.1985,
  author    = {K{\"o}nig, W and Scheffer, J. and Bremm, K. D. and Hacker, J{\"o}rg and Goebel, W.},
  title     = {The role of bacterial adherence and toxin production from E. coli on leukotriene generation from human polymorphonuclear granulocytes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40295},
  year      = {1985},
  abstract  = {No abstract available},
  language  = {en}
}
@article{HackerHofHughesetal.1985,
  author    = {Hacker, J{\"o}rg and Hof, H. and Hughes, C. and Goebel, W.},
  title     = {Salmonella typhimurium strains carrying hemolysin plasmids and cloned hemolysin. genes from Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40309},
  year      = {1985},
  abstract  = {Like all other Salmonella typhimurium strains examined, the smooth variants SF1397 (L T2) and 1366 and also their semi-rough and rough derivatives are non-haemolytic. Nevertheless, two haemolysin (Hly) plasmids of E. coli belonging to the inc groups incFllI,lv (pSU316) and incIz (pHly152) were able to be introduced into these strains by conjugation and stably maintained. A considerable percentage of the Hly+ transconjugants obtained had lost parts of their O-side chains, a result of selection for the better recipient capability of « semi-rough» variants rather than the direct influence of the Hly+ plasmids themselves. In contrast to the incF1lI1V plasmid pSU316, which exhibited higher conjugation rates with rough recipients, the incIz plasmid pHly152 was accepted best by smooth strains. Transformation with cloned E. coli haemolysin (hly) determinant was inefficient ( <10-8) for smooth strains, but 102-103 times higher for rough recipients, and was increased by the use of Salmonella-modified DNA. The transform ants and transconjugants were relatively stable and showed the same haemolytic activity as the E. coli donor strains. The virulence of the Hly+ smooth, semi-rough and rough S. typhimurium strains was tested in two mouse models, and neither the mortality rate nor the ability to multiply within the mouse spleen was influenced by the hly determinants.},
  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{ChakrabortyKathariouHackeretal.1987,
  author    = {Chakraborty, Trinad and Kathariou, Sophia and Hacker, J{\"o}rg and Hof, Herbert and Huhle, Burkhard and Wagner, Wilma and Kuhn, Michael and Goebel, Werner},
  title     = {Molecular analysis of bacterial cytolysins},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40328},
  year      = {1987},
  abstract  = {Results of molecular and pathogenic studies of three different bacterial hemolysins (cytolysins) are presented. These exoproteins derive from the two gram-negative bacteria Escherichia coli and Aeromonas hydrophila and from the gram-positive pathogen Listeria monocytogenes. The hemolysin of E. coli is determined by an 8-kilobase (kb) region that includes four clustered genes (hlyC, hlyA, hlyB, and hlyD). This hemolysin determinant is part either of large transmissible plasmids or of the chromosome. The genes located chromosomally are found predominantly in E. coli strains that can cause pyelonephritis and/or other extraintestinal infections. A detailed analysis of the chromosomal hly determinants of one nephropathogenic E. coli strain revealed the existence of specific, large chromosomal insertions 75 kb and lOO kb in size that carry the hly genes but that also influence the expression of other virulence properties, i.e., adhesion and serum resistance. The direct involvement of E. coli hemolysin in virulence could be demonstrated in several model systems. The genetic determinants for hemolysin (cytolysin) formation in , A. hydrophila (aerolysin) and L. monocytogenes (listeriolysin) are less complex. Both cytolysins seem to be encoded by single genes, although two loci (aerB and aerC) that affect the expression and activity of aerolysin have been identified distal and proximal to the structural gene for aerolysin (aerA). Cytolysin-negative mutants of both bacteria were obtained by site-specific deletion and/or transposon mutagenesis. These mutants show a drastic reduction in the virulence of the respective bacteria.},
  language  = {en}
}
@inproceedings{MochHoschuetzkyHackeretal.1987,
  author    = {Moch, Thomas and Hosch{\"u}tzky, Heinz and Hacker, J{\"o}rg and Kr{\"o}nke, Klaus-D. and Jann, Klaus},
  title     = {Isolation and characterization of the \(\alpha\)-Sialyl-\(\beta\) 2-3-Galactosyl (S)-Specific Adhesin fimbriated Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40330},
  year      = {1987},
  abstract  = {The \(\alpha\)-Sialyl-\(\beta\) 2-3-Galactosyl-specific adhesin (S adhesin) was isolated from cells of a recombinant Escherichia coli K-12 strain expressing the S-flmbrial adhesin complex. A crude cell extract was partiaUy dissociated into fimbriae and an adhesin-enriched fraction by heating to 7O°C. From the latter, adhesin was purified to apparent homogeneity (by fast protein liquid chromatography, immunoblot, and NaDodSO\(_4\)/PAGE) by differential ammonium sulfate precipitation, dissociation in 8 M guanidine hydrochloride, and high-resolution anion-exchange chromatography in 8 M urea. The purified adhesin formed an aggregate of M\(_r\)\(\approx\)10\(^6\) that was made up of one type of 12-kDa polypeptide (fimbrillin is 16.5 kDa). It had pI value of 4.7 (fimbriae has a pI value of 6). Adhesin and fimbrillin had different amino add compositions. The purified adhesins agglutinated human and bovine erythrocytes with the same speclfkity as the whole bacteria; purified fimbriae were not adhesive. Monoclonal anti-adhesin and anti-fimbriae antibodies were obtained. Monoclonal antiadhesin, but none of the anti-fimbriae, antibodies inhibited the agglutination of erythrocytes. The anti-adhesive antibodies were used in immuno-gold electron microscopy to localize adhesin exclusively on the fimbriae, with a possible preference to their tips.},
  language  = {en}
}
@article{WirbelauerHofHacker1988,
  author    = {Wirbelauer, J. and Hof, H. and Hacker, J{\"o}rg},
  title     = {Die Wirkung von Desacetylcefotaxin, einem Metaboliten von Cefotaxim, in vitro und auf die experimentelle Infektion mit Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40348},
  year      = {1988},
  abstract  = {Die MHK-Werte von Desacetylcefotaxim gegen verschiedene, z. T. ampicillinresistente St{\"a}mme von Escherichia coH, die mit Hilfe einer Agardilutionsmethode erhoben wurden, waren h{\"o}her als die von Cefotaxim und Ceftriaxon, jedoch niedriger als die von Cefoxitin. In einem Modell der systemischen Infektion der Maus mit einem plasmidtragenden, betalactamaseproduzierenden Stamm von E. coli f{\"u}hrte die Therapie mit Desacetylcefotaxim zu einer starken Reduktion der Keime pro Leber. Im Vergleich zur Therapie mit Cefotaxim trat die protektive Wirkung aber verlangsamt ein. Desacetylcefotaxim ist also kein unn{\"u}tzes Abbauprodukt von Cefotaxim.},
  language  = {de}
}
@article{VanDieKramerHackeretal.1991,
  author    = {Van Die, I. and Kramer, C. and Hacker, J{\"o}rg and Bergmans, H. and Jongen, W. and Hoekstra, W.},
  title     = {Nucleotide sequence of the genes coding for minor fimbrial subunits of the F1C fimbriae of Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40353},
  year      = {1991},
  abstract  = {F 1 C fimbriae allow uropathogenic Escherichia coli to adhere to specific epithelial surfaces. This adhesive property is probably due to the presence of minor fimbrial components in F1C fimbriae. The foe gene cluster encoding F1C fimbriae has been cloned, as described previously. Here we present the nucleotide sequence (2081 bp) coding for the F 1 C minor fimbria I subunits. The structural genes code for polypeptides of 175 (FocF), 166 (FocG), and 300 (FocH) amino acids. The deduced amino acids of the F 1 C minor subunits were compared with the reported sequences of the minor subunits of other types of fimbriae. The data show that the Foc minor subunits are highly homologous to the corresponding Sfa proteins, whereas homology to the minor subunits of type 1 and P fimbriae is much lower.},
  language  = {en}
}
@article{LueckBenderOttetal.1991,
  author    = {L{\"u}ck, P. Christian and Bender, Larisa and Ott, Manfred and Helbig, J{\"u}rgen H. and Hacker, J{\"o}rg},
  title     = {Analysis of Legionella pneumophila serogroup 6 strains isolated from a hospital warm water supply over a three-year period by using genomic long-range mapping techniques and monoclonal antibodies},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40392},
  year      = {1991},
  abstract  = {Over a period of 3 years, Legionella pneumophila serogroup 6 strains were isolated from warm water outlets and dental units in the Dental Faculty and from the Surgery and Internal Medicine Clinics at the University of Dresden, Dresden, Germany. In the bacteriological unit of the above-mentioned facility, L. pneumophila serogroups 3 and 12 were grown frl,)m warm water specimens. The medical facilities are located in separate buildings connected with a ring pipe warm water system. All L. pneumophila serogroup 6 strains isolated from the warm water supply reacted with a serogroup-specific monoclonal antibody, but not with two other monoclonal antibodies which are subgroup specific, reacting with other serogroup 6 strains. The NolI genomic profiles obtained by pulsed-field gel electrophoresis of 25 serogroup 6 strains isolated from the Dental Faculty over a 3-year period, 1 isolate from the Internal Medicine Clinic, and 4 strains from the Surgery Clinic were identical. Furthermore, all these strains hybridized with a 3OO-kb NolI fragment when a legiolysin (lIy)-specific DNA probe was used. The NolI pattern, however, differed from those of six serogroup 6 strains of other origins, one serogroup 12 strain from the bacteriological unit, and another six unrelated strains of serogroups other than serogroup 6. L. pneumophila serogroup 6 strains which can be divided into only two subgroups by the use of monoclonal antibodies are differentiated in at least six Noli cleavage types obtained by pulsed-field electrophoresis.},
  language  = {en}
}
@article{KuninHuaVanArsdaleWhiteetal.1993,
  author    = {Kunin, Calvin M. and Hua, Tong Hua and Van Arsdale-White, Laura and Krishnan, Chandradekar and Hacker, J{\"o}rg},
  title     = {Isolation of a nicotinamide-requiring clone of Escherichia coli O18:K1:H7 from women with acute cystitis resembles strains found in neonatal meningitis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40406},
  year      = {1993},
  abstract  = {During a study of the nutritional requirements of clinical isolates of Escherichia coli, we found that 21 (7.0\%) of 301 strains required nicotinamide to grow in minimal medium. The nicotinamide- requiring strains were present in 16 (15.8\%) of 101 cultures of urine from young women with acute cystitis, in 5 (5.0\%) of 100 stool specimens from healthy adults, and in none of 100 blood samples from adult patients with bacteremia. Most of the strains belonged to serogroup OI8:KI:H7, were hemolytic, possessed type I fimbriae, and exhibited similar patterns of antibiotic susceptibility. Two of the urinary isolates expressed S fimbriae, and all 16 urinary isolates contained the s/aS homologue gene on their chromosomes. One of the stool isolates contained the s/aS gene. The urinary isolates closely resembled a large clone of E. coli that is reportedly associated with neonatal meningitis and sepsis. It may be possible to detect this and related clones by their requirement for nicotinamide and to screen strains for S fimbriae by relatively inexpensive hemagglutination methods, including the use of avian PI antigens to detect mannose- resistant, non-P-fimbriated E. coli; the agglutination of bovine erythrocytes; and the use of bovine mucin to detect sialyl galactosides in S fimbriae.},
  language  = {en}
}
@article{HackerOttWintermeyeretal.1993,
  author    = {Hacker, J{\"o}rg and Ott, Manfred and Wintermeyer, Eva and Ludwig, Birgit and Fischer, Gunter},
  title     = {Analysis of virulence factors of Legionella pneumophila.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-70620},
  year      = {1993},
  abstract  = {Legionella pneumophila, the causative agent of Legionnaires' disease is a facultative intracellular bacterium, which in the course of human infection multiplies in lung macrophages predominantly manifesting as pneumonia. The natural habitat of Legionella is found in sweet water reservoirs and man-made water systems. Virulent L. pneumophila spontaneously convert to an avirulent status at a high frequency. Genetic approaches have led to the identification of various L. pneumophila genes. The mip (macrophage infectivity potentiator) determinant remains at present the sole established virulence factor. The Mip protein exhibits activity of a peptidyl prolyl cis trans isomerase (PPiase), an enzyme which is able to bind the immunosuppressant FK506 and is involved in protein folding. The recently cloned major outer membrane protein (MOMP) could play a role in the uptake of legionellae by macrophages. Cellular models are useful in studying the intracellular replication of legionellae in eukaryotic cells. Human celllines and protozoan models are appropriate for this purpose. By using U 937 macrophage-like cells and Acanthamoeba castellanii as hosts, we could discriminate virulent and avirulent L. pneumophila variants since only the virulent strain was capable of intracellular growth at 37 oc. By using these systems we further demonstrated that a hemolytic factor cloned and characterized in our laboratory, legiolysin (lly), had no influence on the intracellular growth of L. pneumophila.},
  subject      = {Legionella pneumophila},
  language  = {en}
}
@article{TschaepeBenderOttetal.1992,
  author    = {Tsch{\"a}pe, Helmut and Bender, Larisa and Ott, Manfred and Wittig, Walter and Hacker, J{\"o}rg},
  title     = {Restriction fragments length polymorphism and virulence pattern of the veterinary pathogen Escherichia coli O139:K82:H1},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86131},
  year      = {1992},
  abstract  = {Escherichia coli 0139: K82: H1 strains originating from outbreaks and single cases of oedema disease in pigs were characterized by their genomic restriction fragment length polymorphism (RFLP), their virulence pattern, and by the occurrence as well as the genomic distribution of the determinants for hemolysin (hly) and verotoxins (shiga-like toxins; sltI, sltII). Whereas the RFLPs revealed considerable variation among the E. coli 0139: K82: H1 isolates depending the origin and epidemic source of the strains, the virulence gene slt II was found to be present in nearly all strains in a particular chromosomal region. Similar to RFLPs, the plasmid profiles are useful for epidemiological analysis.},
  subject      = {Escherichia coli},
  language  = {en}
}
@article{MorschhaeuserVetterKorhonenetal.1993,
  author    = {Morschh{\"a}user, Joachim and Vetter, Viktoria and Korhonen, Timo and Uhlin, Bernt Eric and Hacker, J{\"o}rg},
  title     = {Regulation and binding properties of S fimbriae cloned from E. coli strains causing urinary tract infection and meningitis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86140},
  year      = {1993},
  abstract  = {S fimbriae are able to recognize receptor molecules containing sialic acid and are produced by pathogenic E. coli strains causing urinary tract infection and menigitis. In order to characterize the corresponding genetic determinant, termed S fimbrial adhesin ( sfa) gene duster, we have cloned the S-specific genes from a urinary pathogen and from a meningitis isolate. Nine genes are involved in the production of S fimbriae, two of these, sfaB and sfaC code for regulatory proteins being necessary for the expression of S fimbriae. Two promoters, PB and Pc, are located in front of these genes. Transcription of the sfa determinant is influenced by activation of the promotersvia SfaB and SfaC, the action of the H-NS protein and an RNaseE-specific mRNA processing. In addition, a third promoter, P A• located in front of the major subunit gene sfaA, can be activated under special circumstances. Four genes of the sfa determinant code for the subunit-specific proteins, SfaA (16 kda), SfaG (17 kda), SfaS (14 kda) and SfaH (29 kda). It was demonstrated that the protein SfaA is the major subunit protein while SfaS is identical to the sialic-acid-specific adhesin of S fimbriae. The introduction of specific mutations into sfaS revealed that a region of six amino acids of the adhesin which includes two lysine and one arginine residues is involved in the receptor specific interaction of S fimbriae. Additionally, it has been shown that SfaS is necessary for the induction of fimbriation while SfaH plays a role in the stringency of binding of S fimbriae to erythrocytes.},
  subject      = {Escherichia coli},
  language  = {en}
}
@article{SchrotenWolskePlogmannetal.1991,
  author    = {Schroten, Horst and Wolske, Anja and Plogmann, Ricarda and Hanisch, Franz-Georg and Hacker, J{\"o}rg and Uhlenbr{\"u}ck, Gerhard and Wahn, Volker},
  title     = {Binding of cloned S-fimbriated E. coli to human buccal epithelial cells-different inhibition of binding by neonatal saliva and adult saliva.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86291},
  year      = {1991},
  abstract  = {Investigations were carried out on the adhesion of cloned S-fimbriated E. coli, labelled with fluoresceinisothiocyanate (FITC) to human buccal epithelial cells. Fluorescence microscopic analysis revealed binding of bacteria to 75-95\% of epithelial cells. Inhibition experiments with fetuin, a 1-acid glycoprotein and N-acetyl neuraminic acid confirmed the specificity of bacterial binding to sialoglycoproteins. Further studies using saliva as an inhibitor resulted in a 4-5 times stronger binding inhibition by newborn saliva in comparison to adult saliva coinciding with a 4-5 times higher content of total N-acetyl neuraminic acid in samples of newborn saliva. In Western blot analysis sialoglycoprotein bands with a molecular weight >200 kD reacting with wheat germ agglutinin (WGA), were only identified in samples of newborn saliva. These bands are classified as mucins on account of molecular weight and staining. These data suggest that saliva mucins could represent a major defense mechanism against bacterial infections at a stage of ontogeny where the secretory IgAsystem is not yet developed.},
  subject      = {Escherichia coli},
  language  = {en}
}
@article{ParkkinenHackerKorhonen1991,
  author    = {Parkkinen, Jaakko and Hacker, J{\"o}rg and Korhonen, Timo K.},
  title     = {Enhancement of tissue plasminogen activator-catalyzed plasminogen activation by Escherichia coli S fimbriae associated with neonatal septicaemia and meningitis.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-71566},
  year      = {1991},
  abstract  = {The effect of Escherichia coli strains isolated from blood and cerebrospinal fluid of septic infants on plasminogen activation was studied. These strains typically carry a filamentous surface protein, S fimbria, that has formerly been shown to bind to endothelial cells and interact with plasminogen. The bacteria effectively promoted plasminogen activation by tissue plasminogen activator (t-PA) which was inhibited by e-aminocaproic acid. A recombinant strain expressing S fimbriae accelerated t-PAcatalyzed plasminogen activation to a similar extent as did the wild-type strains whereas the nonfimbriate recipient strain had no effect. After incubation with t-PA and plasminogen, the S-fimbriate strain displayed bacterium-bound plasmin activity whereas the nonfimbriate strain did not. Bacterium-associated plasmin generation was also observed with a strain expressing mutagenized S fimbriae that Iack the cell-binding subunit SfaS but not with a strain lacking the major subunit SfaA. Both t-PA and plasminogen bound to purified S fimbriae in a lysine-dependent manner and purified S fimbriae accelerated t-PA-catalyzed plasminogen activation. The results indicate that E. coli S fimbriae form a complex with t-PA and plasminogen which enhances the rate of plasminogen activation and generates bacterium-bound plasmin. This may promote bacterial invasion and persistence in tissues and contribute to the systemic activation of fibrinolysis in septicaemia.},
  subject      = {Escherichia coli},
  language  = {en}
}
@article{HackerOttBlumetal.1992,
  author    = {Hacker, J{\"o}rg and Ott, Manfred and Blum, Gabriele and Marre, Reinhard and Heesemann, J{\"u}rgen and Tsch{\"a}pe, Helmut and Goebel, Werner},
  title     = {Genetics of Escherichia coli uropathogenicity: Analysis of the O6:K15:H31 isolate 536},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-71578},
  year      = {1992},
  abstract  = {E. coli strain 536 (06: K15: H31) isolated from a case of acute pyelonephritis, expresses S-fimbrial adhesins, P-related fimbriae, common type I fimbriae, and hemolysins. The respective chromosomally encoded determinants were cloned by constructing a genomic library of this strain. Furthermore, the strain produces the iron uptake substance, enterocheline, damages HeLa cells, and behaves in a serum-resistant mode. Genetic analysis of spontaneously arising non-hemolytic variants revealed that some of the virulence genes were physically linked to large unstable DNA regions, termed "pathogenicity islands", which were mapped in the respective positions on the E. coli K-12linkage map. By comparing the wild type strain and mutants in in vitro and in vivo assays, virulence features have been evaluated. In addition, a regulatory cross talk between adhesin determinants was found for the wild-type isolate. This particular mode of virulence regulation is missing in the mutant strain.},
  subject      = {Escherichia coli},
  language  = {en}
}