Bacteria-generated PtdIns(3)P Recruits VAMP8 to Facilitate Phagocytosis

doi:10.1111/j.1600-0854.2007.00613.x

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Wiley InterScience

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Volume 8 Issue 10, Pages 1365 - 1374

Published Online: 16 Jun 2007

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Bacteria-generated PtdIns(3)P Recruits VAMP8 to Facilitate Phagocytosis

Shipan Dai ¹ , Ying Zhang ¹ , Thomas Weimbs ² , Michael B Yaffe ³ Daoguo Zhou ^1,*

¹ Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA
² Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA 93106, USA
³ Department of Biology and Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 21329, USA

Correspondence to *Daoguo Zhou, zhoud@purdue.edu

KEYWORDS

invasion • PtdIns(3)P • Salmonella • SopB • VAMP8

ABSTRACT

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.