Journal
TRAFFIC
Volume 8, Issue 10, Pages 1365-1374Publisher
WILEY
DOI: 10.1111/j.1600-0854.2007.00613.x
Keywords
invasion; PtdIns(3)P; Salmonella; SopB; VAMP8
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Funding
- NIGMS NIH HHS [R01 GM066785] Funding Source: Medline
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Salmonella enterica serovar Typhimurium invades non-phagocytic cells by inducing macropinocytosis. SopB is involved in modulating actin dynamics to promote Salmonella-induced invasion. We report here that SopB-generated PtdIns(3)P binds VAMP8/endobrevin to promote efficient bacterial phagocytosis. VAMP8 is recruited to Salmonella-induced macropinosomes in a nocodazole-dependent, but Brefeldin A-independent, manner. We found that VAMP8 directly binds to and colocalizes with PtdIns(3)P. The inositol phosphatase activity of SopB is required for PtdIns(3)P and VAMP8 accumulation, while wortmannin, a specific phosphatidylinositol 3-kinase inhibitor, has no effect. Knockdown of endogenous VAMP8 by small interfering RNA or expression of a truncated VAMP8 (1-79aa) reduces the invasion level of wild-type Salmonella to that of the phosphatase-deficient SopB(C460S) mutant. Our study demonstrates that Salmonella exploit host SNARE proteins and vesicle trafficking to promote bacterial entry.
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