Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Mikula, Kornelia M., Kolodziejczyk, Robert, Goldman, Adrian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2013
Materias:
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
_version_ 1782255054978285568
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
work_keys_str_mv AT mikulakorneliam yersiniainfectiontoolscharacterizationofstructureandfunctionofadhesins
AT kolodziejczykrobert yersiniainfectiontoolscharacterizationofstructureandfunctionofadhesins
AT goldmanadrian yersiniainfectiontoolscharacterizationofstructureandfunctionofadhesins