@article{MollRoellinghoff1991,
  author    = {Moll, Heidrun and R{\"o}llinghoff, Martin},
  title     = {T-cell reactivity to purified lipophosphoglycan from Leishmania major: A model for analysis of the cellular immune response to microbial carbohydrates.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33022},
  year      = {1991},
  abstract  = {The major macromolecule on the surface o/Leishmania majorpromastigotes is a lipophosphoglycan (LPG). This glycoconjugate plays a key role in determining infectivity and survival of para-sites in the mammalian host cell. In addition, L. major LPG is able to induce a host-protective immune response. In this article, we summarise the evidence for recognition of highly purified LPG by T cells and we discuss the potential mechanisms of T-cell Stimulation by this non-protein antigen.},
  language  = {en}
}
@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{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{BogdanMollSolbachetal.1990,
  author    = {Bogdan, Christian and Moll, Heidrun and Solbach, Werner and R{\"o}llinghoff, Martin},
  title     = {Tumor necrosis factor-\(\alpha\) in combination with interferon-\(\gamma\), but not with interleukin 4 activates murine macrophages for elimination of Leishmania major amastigotes},
  volume    = {20},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-31614},
  pages     = {1131 -- 1135},
  year      = {1990},
  abstract  = {We have previously shown that during an infection with Leishmania major, susceptible BALB/c mice, as opposed to mice of a resistant strain (C57BLl6), are primed by lipopolysaccharide for the production of high levels of tumor necrosis factor-\(\alpha\) (TNF-\(\alpha\)) which is known to be a potent maerophage M\(\Phi\) stimulator in other parasitic diseases. In the present study we investigated whether TNF-\(\alpha\) activates M\(\Phi\) for killing of L. major parasites. In the absence of interferon-y (IFN-\(\gamma\)) or lipopolysaccharide, TNF-\(\alpha\) (0.025-25000 U/ml) failed to activate peritoneal exudate M\(\Phi\) from BALB/c mice for killling of L. major amastigotes. In the presence of suboptimal doses of IFN-\(\gamma\) (5 or 10 Vlml), however, TNF-\(\alpha\) mediated a rapid elimination of intracellular parasites, which was highly significant compared to IFN-\(\gamma\) alone. Tbe combination of TNF with interleukin 4, in contrast, was inactive in this respect and allowed survival of intracellular parasites. From these data we conelude that the presence of IFN-\(\gamma\) is crucial for TNF-\(\alpha\)-mediated killing of L. major parasites by M\(\Phi\). Disease progression in susceptible mice therefore seems to be a consequence of a deficiency of IFN-\(\gamma\) and a predominance of interleukin 4 rather than the result of an excess amount of TNF-\(\alpha\).},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{MollBinoederBogdanetal.1990,
  author    = {Moll, Heidrun and Bin{\"o}der, Kerstin and Bogdan, Christian and Solbach, Werner and R{\"o}llinghoff, Martin},
  title     = {Production of tumour necrosis factor during murine cutaneous leishmaniasis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61291},
  year      = {1990},
  abstract  = {We have assessed the role of tumour necrosis factor-a (TNF) during cutaneous leishmaniasis and demonstrated that significant levels of TNF were released by spleen cells from infected mice after in cirro restimulation with Leishmania major promastigotes. Spleen cells from both genetically resistant and genetically susceptible mice were equally capable of producing TNF. After challenge with bacterial endotoxin, TNF activity could also be demonstrated in the serum of L. mujor-infected mice and the titres correlated with the course of cutaneous disease in susceptible and resistant mice. TNF did not exert a direct leishmanicidal effect in uitro. Furthermore, our study indicated that macrophages are the source of L. major-induced TNF activity and that its elicitation is dependent on the presence of T cells. These findings suggest that TNF acts in concert with other cytokines produced during L. major infection and that its role depends on the composition of T cell subsets and cytokines present.},
  subject      = {Immunologie},
  language  = {en}
}
@article{MollRoellinghoff1990,
  author    = {Moll, Heidrun and R{\"o}llinghoff, Martin},
  title     = {Resistance to murine cutaneous leishmaniasis is mediated by T\(_H\)1 cells, but disease-promoting CD4\(^+\) cells are different from T\(_H\)2 cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61305},
  year      = {1990},
  abstract  = {No abstract available},
  subject      = {Biologie},
  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{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{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{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{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{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{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{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}
}
@misc{GillitzerBergerMoll1990,
  author    = {Gillitzer, Reinhard and Berger, Rudolf and Moll, Heidrun},
  title     = {A reliable method for simultaneous demonstration of two antigens using a novel combination of immunogold-silver staining with immunoenzymatic labeling},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-31092},
  year      = {1990},
  abstract  = {We have developed a reliable and sensitive immunohistochemical staining technique which allows the simultaneous demonstration of two different antigens expressed in or on the same cell (referred to as mixed labeling), together with the evaluation of the general histopathological appearance of the tissue. The staining procedure combines a three-step (streptavidin-biotin) immunogold-silver staining (IGSS) with a three-step immunoenzymatic labeling. For this purpose, we investigated the compatibility ofIGSS with various substrates of peroxidase or alkaline phosphatase (AP). Highly reliable and discernible mixed labeling was achieved only after iniriallabeling with IGSS followed by AP labeling using the substrates naphthol AS-MX phosphate/Fast Blue or naphthol AS-HI phosphate/New Fuchsin, respectively. To ensure utmost specificity, we applied FlTC-conjugated mouse monoclonal antibodies and rabbit anti-FlTC immunoglobulins visualized by AP-labeled immunoglobulins and the respective substrate in a final step. This novel approach provides an excellent means for demonstration of immunocompetent cells and unequivocal determination of the percentage of specific cell subsets in infiltrated tissue. The advantages of this method, as compared with double immunofluorescence or double immunoenzymatic labeling, were investigated and are discussed. (J Histochem Cytochem 38:307-313, 1990)},
  language  = {en}
}
@article{HackerGadebergOrskov1989,
  author    = {Hacker, J{\"o}rg and Gadeberg, Ole V. and Orskov, Ida},
  title     = {Role of alpha-Hemolysin for the in vitro Phagocytosis and intracellular killing of Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-73019},
  year      = {1989},
  abstract  = {The_role of a-hemolysin for the elimination of Eschericbia coli by phagocyres in vitro was investigated using sets of isogenic strains which included wild-type a -hemolyric srrains, derived strains with a reduced production of a-hemolysin and derived nonhemolytic strains. Phagocyrosis and intracellular killing of the bacteria by human blood granulocytes or monocytes were measured using growth inhibition rechniques. a-hemolytic strains were phagocytosed and killed ro a Jesser extent than isogenic strains with a reduced production of o:hemoJysin and isogenic nonhemolytic strains. The results obrained with granulocyres were similar to rhose obtained with monocyres although the elimination of bacteria by monocytes was less than that by granulocytes. These resulcs strongJy suggest that production of ahemolysin is a means by which E. coli counteracrs the activity of phagocytes by injuring these cells with the toxin.},
  subject      = {Escherichia coli},
  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{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{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{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{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{MollScollay1989,
  author    = {Moll, Heidrun and Scollay, Roland},
  title     = {L3T4+ T cells promoting susceptibility to murine cutaneous leishmaniasis express the surface marker Ly-24 (Pgp-1)},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61275},
  year      = {1989},
  abstract  = {No abstract available},
  subject      = {Biologie},
  language  = {en}
}
@article{MollMitchellMcConvilleetal.1989,
  author    = {Moll, Heidrun and Mitchell, Graham F. and McConville, Malcom J. and Handman, Emanuela},
  title     = {Evidence for T cell recognition in mice of a purified lipophosphoglycan from Leishmania major},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61288},
  year      = {1989},
  abstract  = {We have previously reported that a Leishmania major lipophosphoglycan (LPG), given with killed Corynebacterium parvum as an adjuvant, can vaccinate mice against cutaneous leishmaniasis. In order to analyze whetber T cells are able to recognize this important parasite antigen, we have studied both humoral and cellular immune responses to L. major LPG that bad been isolated from promastigotes by sequential solvent extraction and bydrophobic chromatography. The data sbow that immunization of mice with highly purified LPG induced an increase in frequency of L. major-reactive T cells and the production of immunoglobulin G antibodies to LPG. Furthermore, genetically resistant mice infected with L. major were able to develop a specific delayed-type hypersensitivity response in the ear to L. major LPG. These findings strongly suggest that T cells can recognize and respond to glycolipid antigens, in this case a bost-protective Leishmania LPG, even though such antigens appear not to be potent T-cell stimulators in mice.},
  subject      = {Biologie},
  language  = {en}
}
@article{SolbachBogdanMolletal.1989,
  author    = {Solbach, W. and Bogdan, C. and Moll, Heidrun and Lohoff, M. and R{\"o}llinghoff, M.},
  title     = {Parasit{\"a}re Evasionsmechanismen: Beispiel Leishmanien},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-30920},
  year      = {1989},
  abstract  = {Leishmanien besitzen eine Vielzahl von Mechanismen, die humorale und zellul{\"a}re Immunabwehr effektiv zu unterlaufen. Diese h{\"a}ngen eng mit der Expression von haupts{\"a}chlich zwei Glykokonjugaten auf der Parasitenoberfl{\"a}che zusammen, dem gp63 und dem Lipophosphoglykan. Die Parasiten sind einerseits schlechte Aktivatoren des alternativen Komplementweges und umgehen damit ihre eigene extrazellul{\"a}re Lyse. Oberfl{\"a}chengebundene Komplementfaktoren f{\"o}rdern andererseits die Aufnahme der Leishmanien durch Makrophagen. Solange diese nicht durch T-Zellen aktiviert sind, dienen sie den Parasiten als "Refugium". Dies gilt insbesondere, als Leishmanien in der Lage sind, 1. den "oxidative burst" zu hemmen; 2. toxische Sauerstoffmetaboliten zu entgiften; 3. abbauende lysosomale Enzyme zu hemmen und 4. das saure Milieu in den Lysosomen f{\"u}r ihren eigenen Metabolismus auszunutzen. Schließlich unterlaufen Leishmanien die zellul{\"a}re Immunabwehr des Wirts, indem sie die Aktivierung von T-Lymphozyten hemmen und die Expansion von T-Zell-Sub-populationen bewirken, die f{\"u}r ihr eigenes {\"U}berleben n{\"u}tzlich sind.},
  language  = {de}
}
@article{TiuDavernGarciaetal.1989,
  author    = {Tiu, W. U. and Davern, K. M. and Garcia, E. G. and Moll, Heidrun and Mitchell, Graham F.},
  title     = {Monoclonal antibodies reacting with Schistosoma japonicum eggs and their target epitopes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-30916},
  year      = {1989},
  abstract  = {Ten monoclonal antibodies (McAbs) raised to Schistosoma japonicum eggs could be assigned using several serological and immunochemical techniques to 3 groups. The McAbs, termed A, B and C-McAbs, apparently recognize carbohydrate epitopes that can be located on the same antigen molecule. The antibodies, generally of IgM isotype, are idiotypically related. They are distinct from another IgM McAb (Group D-McAb) the carbohydrate target epitope of which can also be associated with the epitopes of A. B and C-McAbs. The McAbs produce large vacuolated bleb reactions in the circumoval precipitin test (COPT) and target epitopes have different representations in various life cycle stages such as immature and mature eggs, male and female worms (including S. mansoni). Antigens affinity purified on columns containing A, B, C and D-McAbs stimulate proliferation of T cells from egg-sensitized mice and elicit DTH reactions in such mice. This raises the possibility that the target antigens of these carbohydrate-reactive monoclonal antibodies are immunopathologic and involved in egg-induced granuloma formation.},
  language  = {en}
}
@article{MollBoesingSchneider1988,
  author    = {Moll, Heidrun and B{\"o}sing-Schneider, Rita},
  title     = {The transplantation barrier of nude mice},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-46045},
  year      = {1988},
  abstract  = {Syngeneic memory cells can be stimulated to yield a secondary immune response after their transfer into irradiated euthymie recipients as well as into young thymusless nude mice. It is shown that nude mice older than twelve weeks of age are not permissive towards memory cell activation as it is found in non-irradiated euthymie animals. This barrier to isogeneie or congeneic cells seems to be caused by a pool of cyclophosphamide-sensitive cells. Since young nude mice could be rendered as unpermissive as older nude mice by pretreatment with either PNA-agglutinable thymus cells or nylon-wool passed spleen cells, it is suggested that an increased number of precursor T cells in older nude mice might induce this effect. Further experiments with monoclonal antibodies against the Lyt-l, Lyt-2, and L3T4 marker on T cells indicate that T -helper/inducer activity might be required to establish the "isogeneie barrief" in nude mice.},
  language  = {de}
}
@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{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{MollScollayMitchell1988,
  author    = {Moll, Heidrun and Scollay, R. and Mitchell, G. F.},
  title     = {Resistance to cutaneous leishmaniasis in nude mice injected with L3T4+ T cells but not with Ly-2+ T cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-61269},
  year      = {1988},
  abstract  = {No abstract available},
  subject      = {Biologie},
  language  = {en}
}
@article{MollMitchell1988,
  author    = {Moll, Heidrun and Mitchell, Graham F.},
  title     = {Analysis of variables associated with the promotion of resistance, and its abrogation, in T cell-reconstituted nude mice infected with Leishmania major},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-30949},
  year      = {1988},
  abstract  = {No abstract available},
  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{HackerUlmerFasskeetal.1987,
  author    = {Hacker, J{\"o}rg and Ulmer, E. and Fasske, E. and Schmidt, G.},
  title     = {Isolation and characterization of coliphage Omega18A specific for Escherichia coli O18ac strains},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-73001},
  year      = {1987},
  abstract  = {The bactedophage Q18A, specific for Escherichia coli 018ac srrains, was isolated frorn sewage. The results of host range and conjugation experiments showed that the sensitivity of bacteria to the phage is associated with rhe presence of 018ac antigens. With sorne of rhe 018 strains rhe phage Q18A produces clear Iysis on bacterial lawns only when applied at a high multiplicity and moreover the phage does not multiply. With rhe help of the phage Ql8A, E. coli 0 18ac strains could be divided inro rwo serologically clistinct subgroups called 018A and 018A1• E. coli strains belanging to the sugroup 0 ISAare sensitive to phage Q t8A wheteas bacteria of subgroup A1 are resistanr.},
  subject      = {Escherichia coli},
  language  = {en}
}
@article{HughesHackerDueveletal.1987,
  author    = {Hughes, C. and Hacker, J{\"o}rg and D{\"u}vel, H. and Goebel, W},
  title     = {Chromosomal deletions and rearrangements cause coordinate loss of hemolysis, fimbriation and serum resistance in an uropathogenic strain of Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59470},
  year      = {1987},
  abstract  = {No abstract available},
  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{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{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}
}
@incollection{HandmanMitchellMcConvilleetal.1987,
  author    = {Handman, E. and Mitchell, G. F. and McConville, M. J. and Moll, Heidrun},
  title     = {Towards a carbohydrate-based vaccine against leishmaniasis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33827},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1987},
  abstract  = {No abstract available},
  language  = {en}
}
@article{HackerSchrettenbrunnerSchroeteretal.1986,
  author    = {Hacker, J{\"o}rg and Schrettenbrunner, A. and Schr{\"o}ter, G. and Schmidt, G. and D{\"u}vel, H. and Goebel, W.},
  title     = {Characterization of Escherichia coli wild-type strains by means of agglutination with antisera raised against cloned P-, S- and MS-fimbriae antigens, hemagglutination, serotyping and hemolysin-production},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-72992},
  year      = {1986},
  abstract  = {E. coli stcains isolated from patients with urinary tcact infecrions (UTn very often possess mannose"sensitive (MS) and mannose-resistant (MR) adherence facmrs (fimbriae). According to their receptor specificity the mannose-resistant adhesins can be divided inm several types, P, S, M and X. We have cloned rhe determinants of rhree groups of UTI E. coli adhesins, MS, p and S, and prepared specific aorisera against the fimbriae antigens. 189 hernagglutination (HA+) -positive stcains, 96 fecal isolates and 93 strains isoJated from UTI . have been tesred with rhese specific antisera and further characterized by receptor specific : HA, HA parteras and further of rhe "common 0 serogroups" 01, 02, 04, 06, 07, 08, 018, ' 025, 075, most prevalenr in UTI, and hemolysin production. · 68 (73 \%) of the UTI srrains a.nd 50 (52\%) of the fecal isolates showed P-receptor specificiry; 16 (17\%) of the uropathogenic bacteria and 33 (34\%) of the fecal strains exhibited S, M or X-fimbriae antigens. 24\% of rhe P-hemagglutinating (P+) strains reacted wirb P (F8)-specific antiserum. In contrast, more than three quaner of the s+-srrains were agglutinated by S-specific antiserum. HA-pattern VJ and 018 amigen were found to be associared with P-fimbriae strains, wbereas HA-pattern V and VII and the 0 anrigens 02 (M-type), 06 and 018 (5-type) occurred most frequently in p- -strains. A high percentage of P-fimbriated strains showed mannose-sensitive hemagglurination and hemolysin production.},
  subject      = {Escherichia coli},
  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{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{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{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{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{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}
}