Authors: Stevens, Mark P.¹; Stevens, Joanne M.¹; Jeng, Robert L.²; Taylor, Lowrie A.¹; Wood, Michael W.¹; Hawes, Pippa³; Monaghan, Paul³; Welch, Matthew D.²; Galyov, Edouard E.¹

Source: Molecular Microbiology, Volume 56, Number 1, April 2005 , pp. 40-53(14)

Publisher: Wiley-Blackwell

Abstract:

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.

Document Type: Research article

DOI: http://dx.doi.org/10.1111/j.1365-2958.2004.04528.x

Affiliations: 1: Division of Microbiology, Institute for Animal Health, Compton Laboratory, Berkshire, RG20 7NN, UK. 2: Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA. 3: Bioimaging Department, Institute for Animal Health, Pirbright Laboratory, Surrey, GU24 0NF, UK.

Publication date: 2005-04-01

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• By this author: 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.

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