Legionella effector Lpg1137 shuts down ER-mitochondria communication through cleavage of syntaxin 17

Kohei Arasaki (), Yumi Mikami, Stephanie R. Shames, Hiroki Inoue, Yuichi Wakana and Mitsuo Tagaya ()
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Kohei Arasaki: School of Life Sciences, Tokyo University of Pharmacy and Life Sciences
Yumi Mikami: School of Life Sciences, Tokyo University of Pharmacy and Life Sciences
Stephanie R. Shames: Yale University School of Medicine
Hiroki Inoue: School of Life Sciences, Tokyo University of Pharmacy and Life Sciences
Yuichi Wakana: School of Life Sciences, Tokyo University of Pharmacy and Life Sciences
Mitsuo Tagaya: School of Life Sciences, Tokyo University of Pharmacy and Life Sciences

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: Abstract During infection of macrophages, the pathogenic bacterium Legionella pneumophila secretes effector proteins that induce the conversion of the plasma membrane-derived vacuole into an endoplasmic reticulum (ER)-like replicative vacuole. These ER-like vacuoles are ultimately fused with the ER, where the pathogen replicates. Here we show that the L. pneumophila effector Lpg1137 is a serine protease that targets the mitochondria and their associated membranes. Lpg1137 binds to and cleaves syntaxin 17, a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein that is known to participate in the regulation of mitochondrial dynamics through interaction with the mitochondrial fission factor Drp1 in fed cells and in autophagy through interaction with Atg14L and other SNAREs in starved cells. Cleavage of syntaxin 17 inhibits not only autophagy but also staurosporine-induced apoptosis occurring in a Bax, Drp1-dependent manner. Thus, L. pneumophila can shut down ER–mitochondria communication through cleavage of syntaxin 17.

Date: 2017
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DOI: 10.1038/ncomms15406

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