3eb8 | pdb_00003eb8
VirA
Structural highlights
FunctionVIRA_SHIFL Alpha-tubulin-specific protease that is required for entry into epithelial cells and for subsequent intra- and intercellular spreading. Contributes to bacterial entry into epithelial cells by inducing microtubule (MT) destabilization and the formation of membrane ruffles. The membrane ruffling evoked by VirA results from the activation of host rac1, which is associated with the destruction of MT networks. Creates a tunnel inside the host cell cytoplasm by breaking down the microtubule infrastructure. This facilitates the bacterium's movement through the cytoplasm and also helps other bacteria move faster during the invasion of the eukaryotic cell. Is absolutely required for virulence.[1] [2] [3] Publication Abstract from PubMedVirA, an essential virulence factor in Shigella disease pathogenesis, is involved in the uptake, motility, and cell-to-cell spread of Shigella organisms within the human host. These functions have been attributed to a VirA protease activity and a mechanism of microtubule destruction via tubulin degradation [Yoshida, S., et al. (2006) Science 314, 985-989]. We report functional and crystallographic data indicating a novel VirA structure that lacks these activities but highlights the homology to the EspG virulence factor of pathogenic Escherichia coli. Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules.,Germane KL, Ohi R, Goldberg MB, Spiller BW Biochemistry. 2008 Sep 30;47(39):10241-3. Epub 2008 Sep 3. PMID:18763811[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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