Journal
CELL HOST & MICROBE
Volume 5, Issue 3, Pages 225-233Publisher
CELL PRESS
DOI: 10.1016/j.chom.2009.01.010
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Funding
- Wellcome Trust Program grant (V.K.)
- Medical Research Council [G0500583] Funding Source: researchfish
- MRC [G0500583] Funding Source: UKRI
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Virulence effectors delivered into intestinal epithelial cells by Salmonella trigger actin remodeling to direct pathogen internalization and intracellular replication in Salmonella-containing vacuoles (SCVs). One such effector, SptP, functions early during pathogen entry to deactivate Rho GTPases and reverse pathogen-induced cytoskeletal changes following uptake. SptP also harbors a C-terminal protein tyrosine phosphatase (PTPase) domain with no clear host substrates. Investigating SptP's longevity in infected cells, we uncover a late function of SptP, showing that it associates with SCVs, and its PTPase activity increases pathogen replication. Direct SptP binding and specific dephosphorylation of the AAA+ ATPase valosin-containing protein (VCP/p97), a facilitator of cellular membrane fusion and protein degradation, enhanced pathogen replication in SCVs. VCP and its adaptors p47 and Ufd1 were necessary for generating Salmonella-induced filaments on SCVs, a membrane fusion event characteristic of the pathogen replicative phase. Thus, Salmonella regulates the biogenesis; of an intracellular niche through SptP-mediated dephosphorylation of VCP.
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