Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin

被引:572
作者
Pukatzki, Stefan [1 ]
Ma, Amy T. [1 ]
Revel, Andrew T. [1 ]
Sturtevant, Derek [1 ]
Mekalanos, John J. [1 ]
机构
[1] Harvard Univ, Sch Med, Dept Microbiol & Mol Genet, Boston, MA 02115 USA
关键词
bacteriophage; cytotoxicity; Vibrio cholerae; virulence;
D O I
10.1073/pnas.0706532104
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
Genes encoding type VI secretion systems (T6SS) are widely distributed in pathogenic Gram-negative bacterial species. In Vibrio cholerae, T6SS have been found to secrete three related proteins extracellularly, VgrG-1, VgrG-2, and VgrG-3. VgrG-1 can covalently cross-link actin in vitro, and this activity was used to demonstrate that V. cholerae can translocate VgrG-1 into macrophages by a T6SS-dependent mechanism. Protein structure search algorithms predict that VgrG-related proteins likely assemble into a trimeric complex that is analogous to that formed by the two trimeric proteins gp27 and gp5 that make up the baseplate "tail spike" of Escherichia coli bacteriophage T4. VgrG-1 was shown to interact with itself, VgrG-2, and VgrG-3, suggesting that such a complex does form. Because the phage tail spike protein complex acts as a membrane-penetrating structure as well as a conduit for the passage of DNA into phage-infected cells, we propose that the VgrG components of the T6SS apparatus may assemble a "cellpuncturing device" analogous to phage tail spikes to deliver effector protein domains through membranes of target host cells.
引用
收藏
页码:15508 / 15513
页数:6
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