Structural and Functional Studies Indicate That Shigella VirA Is Not a Protease and Does Not Directly Destabilize Microtubules
- Harvard-MED
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.
- Research Organization:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1006933
- Journal Information:
- Biochemistry-US, Journal Name: Biochemistry-US Journal Issue: (39) ; 2008 Vol. 47; ISSN 0006-2960; ISSN BICHAW
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
Structural and Functional Studies Indicate That the EPEC Effector, EspG, Directly Binds p21-Activated Kinase
Novel fold of VirA, a type III secretion system effector protein from Shigella flexneri
Structurally Distinct Bacterial TBC-like GAPs Link Arf GTPase to Rab1 Inactivation to Counteract Host Defenses
Journal Article
·
Tue Sep 20 00:00:00 EDT 2011
· Biochemistry-US
·
OSTI ID:1023669
Novel fold of VirA, a type III secretion system effector protein from Shigella flexneri
Journal Article
·
Tue Jan 27 23:00:00 EST 2009
· Protein Sci.
·
OSTI ID:1007051
Structurally Distinct Bacterial TBC-like GAPs Link Arf GTPase to Rab1 Inactivation to Counteract Host Defenses
Journal Article
·
Wed Oct 10 00:00:00 EDT 2012
· Cell
·
OSTI ID:1050745