Structural Studies of the Outer Membrane Protein Ail from Y. Pestis

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Resistance of Yersinia pestis to complement-dependent killing is mediated by the Ail outer membrane protein.

Yersinia pestis, the causative agent of plague, must survive in blood in order to cause disease and to be transmitted from host to host by fleas. Members of the Ail/Lom family of outer membrane proteins provide protection from complement-dependent killing for a number of pathogenic bacteria. The Y. pestis KIM genome is predicted to encode four Ail/Lom family proteins. Y. pestis mutants specific...

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The Yersinia pseudotuberculosis outer membrane protein Ail recruits the human complement regulatory protein factor H.

Previous investigations characterizing the mechanism(s) of complement resistance in Yersinia pseudotuberculosis showed that the outer membrane protein Ail can functionally recruit the regulator of the classical and lectin pathways of complement, C4b-binding protein. In this study, we extend these observations and show that Ail can also recruit the regulator of the alternative pathway (AP), fact...

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Yersinia pestis Ail: multiple roles of a single protein

Yersinia pestis is one of the most virulent bacteria identified. It is the causative agent of plague-a systemic disease that has claimed millions of human lives throughout history. Y. pestis survival in insect and mammalian host species requires fine-tuning to sense and respond to varying environmental cues. Multiple Y. pestis attributes participate in this process and contribute to its pathoge...

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Functional recruitment of the human complement inhibitor C4BP to Yersinia pseudotuberculosis outer membrane protein Ail.

Ail is a 17-kDa chromosomally encoded outer membrane protein that mediates serum resistance (complement resistance) in the pathogenic Yersiniae (Yersinia pestis, Y. enterocolitica, and Y. pseudotuberculosis). In this article, we demonstrate that Y. pseudotuberculosis Ail from strains PB1, 2812/79, and YPIII/pIB1 (serotypes O:1a, O:1b, and O:3, respectively) can bind the inhibitor of the classic...

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Ail Proteins of Yersinia pestis and Y. pseudotuberculosis Have Different Cell Binding and Invasion Activities

The Yersinia pestis adhesin Ail mediates host cell binding and facilitates delivery of cytotoxic Yop proteins. Ail from Y. pestis and Y. pseudotuberculosis is identical except for one or two amino acids at positions 43 and 126 depending on the Y. pseudotuberculosis strain. Ail from Y. pseudotuberculosis strain YPIII has been reported to lack host cell binding ability, thus we sought to determin...

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ژورنال

عنوان ژورنال: Biophysical Journal

سال: 2012

ISSN: 0006-3495

DOI: 10.1016/j.bpj.2011.11.1450