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

DOI Web Site 17 Citations
  • Amy D. B. Liverman
    Department of Molecular Biology and
  • Hui-Chun Cheng
    Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75390
  • Jennifer E. Trosky
    Department of Molecular Biology and
  • Daisy W. Leung
    Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75390
  • Melanie L. Yarbrough
    Department of Molecular Biology and
  • Dara L. Burdette
    Department of Molecular Biology and
  • Michael K. Rosen
    Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75390
  • Kim Orth
    Department of Molecular Biology and

Description

<jats:p> Microbial pathogens use a variety of mechanisms to disrupt the actin cytoskeleton during infection. <jats:italic>Vibrio parahaemolyticus</jats:italic> ( <jats:italic>V. para</jats:italic> ) is a Gram-negative bacterium that causes gastroenteritis, and new pandemic strains are emerging throughout the world. Analysis of the <jats:italic>V. para</jats:italic> 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 <jats:italic>V. para</jats:italic> induces the formation of long actin fibers in a VopL-dependent manner. Transfection of VopL promotes the assembly of actin stress fibers. <jats:italic>In vitro</jats:italic> , recombinant VopL potently induces assembly of actin filaments that grow at their barbed ends, independent of eukaryotic factors. <jats:italic>Vibrio</jats:italic> VopL is predicted to be a bacterial virulence factor that disrupts actin homeostasis during an enteric infection of the host. </jats:p>

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