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Vibrio effector protein, VopQ, forms a lysosomal gated channel that disrupts host ion homeostasis and autophagic flux
Anju Sreelatha, Terry L. Bennett, Hui Zheng, Qiu-Xing Jiang, Kim Orth and Vincent J. Starai
Proceedings of the National Academy of Sciences of the United States of America
Vol. 110, No. 28 (July 9, 2013), pp. 11559-11564
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/42712772
Page Count: 6
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Defects in normal autophagic pathways are implicated in numerous human diseases—such as neurodegenerative diseases, cancer, and cardiomyopathy—highlighting the importance of autophagy and its proper regulation. Herein we show that Vibrio parahaemolyticus uses the type III effector VopQ (Vibrio outer protein Q) to alter autophagic flux by manipulating the partitioning of small molecules and ions in the lysosome. This effector binds to the conserved Vo domain of the vacuolar-type H+ -ATPase and causes deacidification of the lysosomes within minutes of entering the host cell. VopQ forms a gated channel ~18 Å in diameter that facilitates outward flux of ions across lipid bilayers. The electrostatic interactions of this type 3 secretion system effector with target membranes dictate its preference for host vacuolar-type H+ -ATPase-containing membranes, indicating that its pore-forming activity is specific and not promiscuous. As seen with other effectors, VopQ is exploiting a eukaryotic mechanism, in this case manipulating lysosomal homeostasis and autophagic flux through transmembrane permeation.
Proceedings of the National Academy of Sciences of the United States of America © 2013 National Academy of Sciences