4.8 Article

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

Publisher

NATL ACAD SCIENCES
DOI: 10.1073/pnas.0703196104

Keywords

actin assembly; microbial pathogenesis; virulence; stress fibers; WH2 domains

Funding

  1. NIAID NIH HHS [R01 AI056404, R01 AI 056404] Funding Source: Medline
  2. NIDDK NIH HHS [R21 DK 072134, R21 DK072134] Funding Source: Medline
  3. NIGMS NIH HHS [T32 GM 08203-18, R01 GM 056322, P01 GM 066311, R01 GM056322, T32 GM008203, P01 GM066311] Funding Source: Medline

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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.

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