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Identification of a bacterial factor required for actin‐based motility of Burkholderia pseudomallei
Author(s) -
Stevens Mark P.,
Stevens Joanne M.,
Jeng Robert L.,
Taylor Lowrie A.,
Wood Michael W.,
Hawes Pippa,
Monaghan Paul,
Welch Matthew D.,
Galyov Edouard E.
Publication year - 2005
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2004.04528.x
Subject(s) - biology , burkholderia pseudomallei , actin , microbiology and biotechnology , bacterial adhesin , cytoplasm , actin binding protein , actin cytoskeleton , cytoskeleton , bacteria , cell , biochemistry , gene , genetics , escherichia coli
Summary Burkholderia pseudomallei is a Gram‐negative facultative intracellular pathogen that enters and escapes from eukaryotic cells using the power of actin polymerization. We have identified a bacterial protein (BimA) that is required for the ability of B. pseudomallei to induce the formation of actin tails. BimA contains proline‐rich motifs and WH2‐like domains and shares limited homology at the C‐terminus with the Yersinia autosecreted adhesin YadA. BimA is located at the pole of the bacterial cell at which actin polymerization occurs and mutation of bimA abolished actin‐based motility of the pathogen in J774.2 cells. Transient expression of BimA in HeLa cells resulted in F‐actin clustering reminiscent of that seen on WASP overexpression. Antibody‐mediated clustering of a CD32 chimera in which the cytoplasmic domain was replaced with BimA resulted in localization of the chimera to the tips of F‐actin enriched membrane protrusions. We report that purified truncated BimA protein binds monomeric actin in a concentration‐dependent manner in cosedimentation assays and that BimA stimulates actin polymerization in vitro in a manner independent of the cellular Arp2/3 complex.

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