Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules

被引：27

作者：

Germane, Katherine L. ^{[1
,2
,3
]}

Ohi, Ryoma ^{[1
,2
,3
]}

Goldberg, Marcia B. ^{[4
,5
]}

Spiller, Benjamin W. ^{[1
,2
,3
]}

机构：

[1] Vanderbilt Univ, Med Ctr, Dept Pharmacol, Nashville, TN 37232 USA

[2] Vanderbilt Univ, Med Ctr, Dept Microbiol & Immunol, Nashville, TN 37232 USA

[3] Vanderbilt Univ, Med Ctr, Dept Cell & Dev Biol, Nashville, TN 37232 USA

[4] Massachusetts Gen Hosp, Cambridge, MA 02139 USA

[5] Harvard Univ, Sch Med, Cambridge, MA 02139 USA

来源：

BIOCHEMISTRY | 2008年 / 47卷 / 39期

关键词：

D O I：

10.1021/bi801533k

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：10241 / 10243

页数：3

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