SdhA blocks disruption of the Legionella-containing vacuole by hijacking the OCRL phosphatase
Won Young Choi, Seongok Kim, Philipp Auraß, Wenwen Huo, Elizabeth A. Creasey, Marc Edwards, Martin Lowe, Ralph R. Isberg
Abstract
), and interfering with endosomal trafficking. SdhA interrupts Rab guanosine triphosphatase (GTPase)-OCRL interactions by binding to the OCRL ASPM-SPD2-Hydin (ASH) domain, without directly altering OCRL 5-phosphatase activity. The Legionella vacuole encompassing the sdhA mutant accumulates OCRL and endosomal antigen EEA1 (Early Endosome Antigen 1), consistent with SdhA blocking accumulation of OCRL-containing endosomal vesicles. Therefore, SdhA hijacking of OCRL is associated with blocking trafficking events that disrupt the pathogen vacuole.
Topics & Concepts
SDHAVacuoleCell biologyEndosomeBiologyBiochemistryIntracellularCytoplasmSuccinate dehydrogenaseMitochondrionLegionella and Acanthamoeba researchBiomedical Research and PathophysiologyNeutrophil, Myeloperoxidase and Oxidative Mechanisms