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Arp2/3-independent assembly of actin by Vibrio type III effector VopL
Journal article

Arp2/3-independent assembly of actin by Vibrio type III effector VopL

Amy D. B. Liverman, Hui-Chun Cheng, Jennifer E. Trosky, Daisy W. Leung, Melanie L. Yarbrough, Dara L. Burdette, Michael K. Rosen and Kim Orth
Proceedings of the National Academy of Sciences of the United States of America, Vol.104(43), pp.17117-17122
23/10/2007

Abstract

Actin assembly Microbial pathogenesis Stress fibers Virulence WH2 domains
Microbial pathogens use a variety of mechanisms to disrupt the actin cytoskeleton during infection. Vibrio parahaemolyticus (V. para) is a Gram-negative bacterium that causes gastroenteritis, and new pandemic strains are emerging throughout the world. Analysis of the V. para genome revealed a type III secretion system effector, VopL, encoding three Wiskott-Aldrich homology 2 domains that are interspersed with three proline-rich motifs. Infection of HeLa cells with V. para induces the formation of long actin fibers in a VopL-dependent manner. Transfection of VopL promotes the assembly of actin stress fibers. In vitro, recombinant VopL potently induces assembly of actin filaments that grow at their barbed ends, independent of eukaryotic factors. Vibrio VopL is predicted to be a bacterial virulence factor that disrupts actin homeostasis during an enteric infection of the host. © 2007 by The National Academy of Sciences of the USA.

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