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Listeria, Rickettsia, Burkholderia, Shigella and Mycobacterium species subvert cellular actin dynamics to facilitate their movement within the host cytosol and to infect neighbouring cells while evading host immune surveillance and promoting their intracellular survival. 'Attaching and effacing' Escherichia coli do not enter host cells but attach intimately to the cell surface, inducing motile actin-rich pedestals, the function of which is currently unclear. The molecular basis of actin-based motility of these bacterial pathogens reveals novel insights about bacterial pathogenesis and fundamental host-cell pathways. [ABSTRACT FROM AUTHOR]

Recently we identified a bacterial factor (BimA) required for actin-based motility of Burkholderia pseudomallei. Here we report that Burkholderia mallei and Burkholderia thailandensis are capable of actin-based motility in J774.2 cells and that BimA homologs of these bacteria can restore the actin-based motility defect of a B. pseudomallei bimA mutant. While the BimA homologs differ in their amino-terminal sequence, they interact directly with actin in vitro and vary in their ability to bind Arp3. [ABSTRACT FROM AUTHOR]

Burkholderia pseudomalleiis 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 ofB. pseudomalleito induce the formation of actin tails. BimA contains proline-rich motifs and WH2-like domains and shares limited homology at the C-terminus with theYersiniaautosecreted adhesin YadA. BimA is located at the pole of the bacterial cell at which actin polymerization occurs and mutation ofbimAabolished 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 polymerizationin vitroin a manner independent of the cellular Arp2/3 complex. [ABSTRACT FROM AUTHOR]