Yersinia infection tools-characterization of structure and function of adhesins

75Citations
Citations of this article
140Readers
Mendeley users who have this article in their library.

Abstract

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, ß1 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 ß-barrel composed of 8, 10, or 12 antiparallel ß-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 ß-strands in the ß-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. © 2013 Mikula, Kolodziejczyk and Goldman.

Cite

CITATION STYLE

APA

Mikula, K. M., Kolodziejczyk, R., & Goldman, A. (2013). Yersinia infection tools-characterization of structure and function of adhesins. Frontiers in Cellular and Infection Microbiology. Frontiers Media S.A. https://doi.org/10.3389/fcimb.2012.00169

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free