Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules.
Publication Type:Journal Article
Source:Biochemistry, Volume 47, Issue 39, p.10241-3 (2008)
Keywords:Bacterial Proteins, Dysentery, Bacillary, Escherichia coli Proteins, Humans, Microtubules, Models, Molecular, Papain, Protein Conformation, Shigella, Tubulin, Virulence Factors
<p>VirA, 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.</p>