@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{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{SzalayHillStritzkeretal.2011,
  author    = {Szalay, Aladar A. and Hill, Philip J. and Stritzker, Jochen and Scadeng, Miriam and Geissinger, Ulrike and Haddad, Daniel and Basse-L{\"u}sebrink, Thomas C. and Gbureck, Uwe and Jakob, Peter},
  title     = {Magnetic Resonance Imaging of Tumors Colonized with Bacterial Ferritin-Expressing Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-75789},
  year      = {2011},
  abstract  = {Background: Recent studies have shown that human ferritin can be used as a reporter of gene expression for magnetic resonance imaging (MRI). Bacteria also encode three classes of ferritin-type molecules with iron accumulation properties. Methods and Findings: Here, we investigated whether these bacterial ferritins can also be used as MRI reporter genes and which of the bacterial ferritins is the most suitable reporter. Bacterial ferritins were overexpressed in probiotic E. coli Nissle 1917. Cultures of these bacteria were analyzed and those generating highest MRI contrast were further investigated in tumor bearing mice. Among members of three classes of bacterial ferritin tested, bacterioferritin showed the most promise as a reporter gene. Although all three proteins accumulated similar amounts of iron when overexpressed individually, bacterioferritin showed the highest contrast change. By site-directed mutagenesis we also show that the heme iron, a unique part of the bacterioferritin molecule, is not critical for MRI contrast change. Tumor-specific induction of bacterioferritin-expression in colonized tumors resulted in contrast changes within the bacteria-colonized tumors. Conclusions: Our data suggest that colonization and gene expression by live vectors expressing bacterioferritin can be monitored by MRI due to contrast changes},
  subject      = {Escherichia coli},
  language  = {en}
}
@article{SebaldArendsMcCarthy1984,
  author    = {Sebald, Walter and Arends, Hermann and McCarthy, John E. G.},
  title     = {Isolation and manipulation of genes coding for energy-transducing enzymes from Neurospora crassa and Escherichia coli},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-86768},
  year      = {1984},
  abstract  = {No abstract available.},
  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{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{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{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{OttHacker1991,
  author    = {Ott, M. and Hacker, J{\"o}rg},
  title     = {Analysis of the variability of S fimbriae expression in an Escherichia coli pathogen.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59695},
  year      = {1991},
  abstract  = {The uropathogenic Escherichia coli wiJd..:type strain 536 produces S-fimbriae, P-related fimbriae and type I fimbriae. Using immuno-colony dot and ELISA techniques, variants were detected showing an increased degree of S-fimbrial production. It was demonstrated by itrtmunofluorescence microscopy that in noimal (wild-type) and hyperS- fimbriated E. coli populaiions non-fimbriated cells also · exist, and that the percentage of Sfinibrlated and non-fimbriated bacteria was roughly identica1 in either population. Hyper-Sfimbriated variants could be stably maintained. The transition from wild-type to hyper-S-fimbriation, which occurs spontaneously, is markedly higher than vice versa. Southern blot analysis of the S fimbrial adhesin (sfa) determinants of normal and hyper-fimbriated strains revealed no marked difference in the gene structure.},
  subject      = {Infektionsbiologie},
  language  = {en}
}
@article{OkoroBarquistConnoretal.2015,
  author    = {Okoro, Chinyere K. and Barquist, Lars and Connor, Thomas R. and Harris, Simon R. and Clare, Simon and Stevens, Mark P. and Arends, Mark J. and Hale, Christine and Kane, Leanne and Pickard, Derek J. and Hill, Jennifer and Harcourt, Katherine and Parkhill, Julian and Dougan, Gordon and Kingsley, Robert A.},
  title     = {Signatures of adaptation in human invasive Salmonella Typhimurium ST313 populations from sub-Saharan Africa},
  series = {PLoS Neglected Tropical Diseases},
  volume    = {9},
  journal   = {PLoS Neglected Tropical Diseases},
  number    = {3},
  doi       = {10.1371/journal.pntd.0003611},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-143779},
  pages     = {e0003611},
  year      = {2015},
  abstract  = {Two lineages of Salmonella enterica serovar Typhimurium (S. Typhimurium) of multi-locus sequence type ST313 have been linked with the emergence of invasive Salmonella disease across sub-Saharan Africa. The expansion of these lineages has a temporal association with the HIV pandemic and antibiotic usage. We analysed the whole genome sequence of 129 ST313 isolates representative of the two lineages and found evidence of lineage-specific genome degradation, with some similarities to that observed in S. Typhi. Individual ST313 S. Typhimurium isolates exhibit a distinct metabolic signature and modified enteropathogenesis in both a murine and cattle model of colitis, compared to S. Typhimurium outside of the ST313 lineages. These data define phenotypes that distinguish ST313 isolates from other S. Typhimurium and may represent adaptation to a distinct pathogenesis and lifestyle linked to an-immuno-compromised human population.},
  language  = {en}
}