Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms

被引：91

作者：

Lilic, M

Galkin, VE

Orlova, A

VanLoock, MS

Egelman, EH

Stebbins, CE

机构：

[1] Rockefeller Univ, Lab Struct Microbiol, New York, NY 10021 USA

[2] Univ Virginia, Hlth Sci Ctr, Dept Biochem & Mol Genet, Charlottesville, VA 22908 USA

来源：

SCIENCE | 2003年 / 301卷 / 5641期

关键词：

D O I：

10.1126/science.1088433

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Like many bacterial pathogens, Salmonella spp. use a type III secretion system to inject virulence proteins into host cells. The Salmonella invasion protein A ( SipA) binds host actin, enhances its polymerization near adherent extracellular bacteria, and contributes to cytoskeletal rearrangements that internalize the pathogen. By combining x-ray crystallography of SipA with electron microscopy and image analysis of SipA-actin. laments, we show that SipA functions as a "molecular staple," in which a globular domain and two nonglobular "arms" mechanically stabilize the. lament by tethering actin subunits in opposing strands. Deletion analysis of the tethering arms provides strong support for this model.

引用

页码：1918 / 1921

页数：4

共 18 条

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