期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 34, 页码 13567-13572出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1207903109
关键词
phosphoinositide signaling; phagocytosis; membrane trafficking; type IV secretion system; virulence factor
资金
- Cornell startup fund
- National Institutes of Health (NIH) [R01-GM094347, K02AI085403, R21AI092043]
- National Science Foundation
- NIH/National Institute of General Medical Sciences via National Science Foundation [DMR-0225180]
- NIH/National Center for Research Resources [RR-01646]
Legionella pneumophila is an opportunistic intracellular pathogen that causes sporadic and epidemic cases of Legionnaires' disease. Emerging data suggest that Legionella infection involves the subversion of host phosphoinositide (PI) metabolism. However, how this bacterium actively manipulates PI lipids to benefit its infection is still an enigma. Here, we report that the L. pneumophila virulence factor SidF is a phosphatidylinositol polyphosphate 3-phosphatase that specifically hydrolyzes the D3 phosphate of PI(3,4)P-2 and PI(3,4,5)P-3. This activity is necessary for anchoring of PI(4)P-binding effectors to bacterial phagosomes. Crystal structures of SidF and its complex with its substrate PI(3,4)P-2 reveal striking conformational rearrangement of residues at the catalytic site to form a cationic pocket that specifically accommodates the D4 phosphate group of the substrate. Thus, our findings unveil a unique Legionella PI phosphatase essential for the establishment of lipid identity of bacterial phagosomes.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据