Identification of a bacterial factor required for actin-based motility of Burkholderia pseudomallei

M P Stevens, J M Stevens, R L Jeng, L A Taylor, M W Wood, P Hawes, P Monaghan, M D Welch, E E Galyov

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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.

Original languageEnglish
Pages (from-to)40-53
Number of pages14
JournalMolecular Microbiology
Volume56
Issue number1
DOIs
Publication statusPublished - Apr 2005

Keywords / Materials (for Non-textual outputs)

  • actins
  • Amino Acid Sequence
  • Bacterial Proteins
  • Burkholderia pseudomallei
  • Cell Line
  • Gene Expression
  • HeLa Cells
  • HUMANS
  • Microfilament Proteins
  • Molecular Sequence Data
  • MOVEMENT
  • Mutation
  • Proline

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