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Vaccinia virus p37 interacts with host proteins associated with LE-derived transport vesicle biogenesis

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Author(s): Chen Yali | Honeychurch Kady | Yang Guang | Byrd Chelsea | Harver Chris | Hruby Dennis | Jordan Robert

Journal: Virology Journal
ISSN 1743-422X

Volume: 6;
Issue: 1;
Start page: 44;
Date: 2009;
Original page

ABSTRACT
Abstract Background Proteins associated with the late endosome (LE) appear to play a central role in the envelopment of a number of taxonomically diverse viruses. How viral proteins interact with LE-associated proteins to facilitate envelopment is not well understood. LE-derived transport vesicles form through the interaction of Rab9 GTPase with cargo proteins, and TIP47, a Rab9-specific effector protein. Vaccinia virus (VV) induces a wrapping complex derived from intracellular host membranes to envelope intracellular mature virus particles producing egress-competent forms of virus. Results We show that VV p37 protein associates with TIP47-, Rab9-, and CI-MPR-containing membranes. Mutation of a di-aromatic motif in p37 blocks association with TIP47 and inhibits plaque formation. ST-246, a specific inhibitor of p37 function, inhibits these interactions and also blocks wrapped virus particle formation. Vaccinia virus expressing p37 variants with reduced ST-246 susceptibility associates with Rab9 and co-localizes with CI-MPR in the presence and absence of compound. Conclusion These results suggest that p37 localizes to the LE and interacts with proteins associated with LE-derived transport vesicle biogenesis to facilitate assembly of extracellular forms of virus.

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Tangokurs Rapperswil-Jona

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