A repeat unit of Vibrio diarrheal T3S effector subverts cytoskeletal actin homeostasis via binding to interstrand region of actin filaments.

ABSTRACT: A novel bacterial type III secretion effector, VopV, from the enteric pathogen Vibrio parahaemolyticus has been identified as a key factor in pathogenicity due to its interaction with cytoskeletal actin. One of the repeat units in the long repetitive region of VopV, named VopV(rep1), functions as an actin-binding module. Despite its importance in pathogenesis, the manner in which the effector binds to actin and the subsequent effects on actin dynamics remain unclear. Here, we report the molecular basis of the VopV(rep1)/actin interaction. VopV(rep1) exists as an unstructured protein in solution but potently and specifically binds filamentous actin (F-actin) and not globular actin (G-actin). The F-actin/VopV(rep1) complex was directly visualized at 9.6-Å resolution using electron cryomicros

SUBMITTER: Nishimura M 

PROVIDER: S-EPMC4650670 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature