Cited by 141Yersinia bacterium, plague, ectoparasites researchEscherichia coli research studiesMicrobial infections and disease research

Plasmid-mediated surface fibrillae of Yersinia pseudotuberculosis and Yersinia enterocolitica: relationship to the outer membrane protein YOP1 and possible importance for pathogenesis

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Kapperud, G, Namork, E, Skurnik, M, Nesbakken, T·1987·Infection and Immunity

Abstract

The cell surface properties of Yersinia pseudotuberculosis and Yersinia enterocolitica mutants, constructed by insertional inactivation of genes located on the 40- to 50-megadalton virulence plasmid, were examined. Electron microscopy revealed an absolute correlation between expression of four plasmid-dependent, temperature-inducible properties related to the bacterial surface: (i) a fibrillar matrix covering the outer membrane, (ii) outer membrane protein YOP1, (iii) spontaneous autoagglutination, and (iv) mannose-resistant hemagglutination of guinea pig erythrocytes. Immunoelectron microscopy indicated that YOP1 is a structural component of the fibrillae. Experiments demonstrating inhibition of hemagglutination by anti-YOP1 monoclonal antibody suggested a potential role for YOP1 in adhesion. Insertional inactivation of the gene coding for YOP1, with resultant loss of the ability to express fibrillae, led to a significant reduction in the capacity of Y. enterocolitica, but not Y. pseudotuberculosis, to colonize the ileum of orogastrically infected mice. In both Y. enterocolitica and Y. pseudotuberculosis, inactivation of the genes coding for Ca2+ dependency reduced the ability to maintain intestinal colonization, regardless of the ability to express fibrillae. Both surface fibrillae and Ca2+ dependency seem to reflect pathogenic determinants which are required for the establishment of Y. enterocolitica infection. In Y. pseudotuberculosis, however, no clinical significance of the fibrillae has so far been defined.

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Crossref · 10.1128/iai.55.9.2247-2254.1987

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  • YadA is expressed at mammalian body temperatures and is exclusively responsible for autoaggregation in Y. enterocolitica and Y. pseudotuberculosis grown at 37 °C.

    “YadA is expressed at mammalian body temperatures and is exclusively responsible for autoaggregation in Y. enterocolitica and Y. pseudotuberculosis grown at 37 °C [148].”

    From Bacterial autoaggregation (2018) · cites this paper as [148]

    The abstract (p. 2247) reports that YOP1 expression and spontaneous autoagglutination are correlated temperature-inducible properties in both species. It does not name YadA, specify growth at 37 °C, or establish that one protein is exclusively responsible for autoaggregation. (LLM, conf=0.84)

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Authors
Kapperud, G., Namork, E., Skurnik, M., & Nesbakken, T.
Venue
Infection and Immunity
Published
1987-09
Volume
55
Issue
9
Pages
2247-2254
ISSN
  • 0019-9567 (ISSN-L)
  • 1098-5522
OpenAlex
W1930066700
Cited by
141
References
1
Citations by year
2018: 2 · 2017: 1 · 2016: 2 · 2015: 1 · 2014: 3 · 2013: 1 · 2012: 3
FWCI
3.69
Type
journal article
Language
en
Open access
Locations
  • Infection and Immunity (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Yersinia bacterium, plague, ectoparasites research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
  • Life Sciences › Immunology and Microbiology › Microbiology › Microbial infections and disease research
Keywords
Yersinia pseudotuberculosis, Yersinia enterocolitica, outer membrane proteins, virulence plasmid, insertional inactivation, autoagglutination, mannose-resistant hemagglutination, bacterial adhesion, intestinal colonization, pathogenesis, monoclonal antibodies
MeSH terms
Agglutinins, Animals, Bacterial Adhesion, Bacterial Outer Membrane Proteins, Calcium, Hemagglutinins, Microscopy, Electron, Mutation, Fimbriae, Bacterial, Plasmids, Yersinia enterocolitica, Yersinia pseudotuberculosis, Mice

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