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Yersinia infection tools—characterization of structure and function of adhesins
Among the seventeen species of the Gram-negative genus Yersinia, three have been shown to be virulent and pathogenic to humans and animals—Y. enterocolitica, Y. pseudotuberculosis, and Y. pestis. In order to be so, they are armoured with various factors that help them adhere to tissues and organelle...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3539135/ https://www.ncbi.nlm.nih.gov/pubmed/23316485 http://dx.doi.org/10.3389/fcimb.2012.00169 |
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author | Mikula, Kornelia M. Kolodziejczyk, Robert Goldman, Adrian |
author_facet | Mikula, Kornelia M. Kolodziejczyk, Robert Goldman, Adrian |
author_sort | Mikula, Kornelia M. |
collection | PubMed |
description | Among the seventeen species of the Gram-negative genus Yersinia, three have been shown to be virulent and pathogenic to humans and animals—Y. enterocolitica, Y. pseudotuberculosis, and Y. pestis. In order to be so, they are armoured with various factors that help them adhere to tissues and organelles, cross the cellular barrier and escape the immune system during host invasion. The group of proteins that mediate pathogen–host interactions constitute adhesins. Invasin, Ail, YadA, YadB, YadC, Pla, and pH 6 antigen belong to the most prominent and best-known Yersinia adhesins. They act at different times and stages of infection complementing each other by their ability to bind a variety of host molecules such as collagen, fibronectin, laminin, β1 integrins, and complement regulators. All the proteins are anchored in the bacterial outer membrane (OM), often forming rod-like or fimbrial-like structures that protrude to the extracellular milieu. Structural studies have shown that the anchor region forms a β-barrel composed of 8, 10, or 12 antiparallel β-strands. Depending on the protein, the extracellular part can be composed of several domains belonging to the immunoglobulin fold superfamily, or form a coiled-coil structure with globular head domain at the end, or just constitute several loops connecting individual β-strands in the β-barrel. Those extracellular regions define the activity of each adhesin. This review focuses on the structure and function of these important molecules, and their role in pathogenesis. |
format | Online Article Text |
id | pubmed-3539135 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-35391352013-01-11 Yersinia infection tools—characterization of structure and function of adhesins Mikula, Kornelia M. Kolodziejczyk, Robert Goldman, Adrian Front Cell Infect Microbiol Microbiology Among the seventeen species of the Gram-negative genus Yersinia, three have been shown to be virulent and pathogenic to humans and animals—Y. enterocolitica, Y. pseudotuberculosis, and Y. pestis. In order to be so, they are armoured with various factors that help them adhere to tissues and organelles, cross the cellular barrier and escape the immune system during host invasion. The group of proteins that mediate pathogen–host interactions constitute adhesins. Invasin, Ail, YadA, YadB, YadC, Pla, and pH 6 antigen belong to the most prominent and best-known Yersinia adhesins. They act at different times and stages of infection complementing each other by their ability to bind a variety of host molecules such as collagen, fibronectin, laminin, β1 integrins, and complement regulators. All the proteins are anchored in the bacterial outer membrane (OM), often forming rod-like or fimbrial-like structures that protrude to the extracellular milieu. Structural studies have shown that the anchor region forms a β-barrel composed of 8, 10, or 12 antiparallel β-strands. Depending on the protein, the extracellular part can be composed of several domains belonging to the immunoglobulin fold superfamily, or form a coiled-coil structure with globular head domain at the end, or just constitute several loops connecting individual β-strands in the β-barrel. Those extracellular regions define the activity of each adhesin. This review focuses on the structure and function of these important molecules, and their role in pathogenesis. Frontiers Media S.A. 2013-01-08 /pmc/articles/PMC3539135/ /pubmed/23316485 http://dx.doi.org/10.3389/fcimb.2012.00169 Text en Copyright © 2013 Mikula, Kolodziejczyk and Goldman. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc. |
spellingShingle | Microbiology Mikula, Kornelia M. Kolodziejczyk, Robert Goldman, Adrian Yersinia infection tools—characterization of structure and function of adhesins |
title | Yersinia infection tools—characterization of structure and function of adhesins |
title_full | Yersinia infection tools—characterization of structure and function of adhesins |
title_fullStr | Yersinia infection tools—characterization of structure and function of adhesins |
title_full_unstemmed | Yersinia infection tools—characterization of structure and function of adhesins |
title_short | Yersinia infection tools—characterization of structure and function of adhesins |
title_sort | yersinia infection tools—characterization of structure and function of adhesins |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3539135/ https://www.ncbi.nlm.nih.gov/pubmed/23316485 http://dx.doi.org/10.3389/fcimb.2012.00169 |
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