Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.

  title={Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.},
  author={FoSheng Hsu and Wenhan Zhu and Lucy C Brennan and Lili Tao and Zhao-Qing Luo and Yuxin Mao},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={109 34},
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… CONTINUE READING


Publications citing this paper.
Showing 1-10 of 31 extracted citations

Molecular Mechanisms in Legionella Pathogenesis

Current Topics in Microbiology and Immunology • 2014
View 5 Excerpts
Highly Influenced

Phosphoinositide lipids and the Legionella pathogen vacuole.

Current topics in microbiology and immunology • 2013
View 7 Excerpts
Highly Influenced


Publications referenced by this paper.
Showing 1-10 of 43 references

Crystal structure of the yeast Sac1: Implications for its phosphoinositide phosphatase function

A Manford
EMBO J 29:1489–1498 • 2010

Similar Papers

Loading similar papers…