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Virol J. 2009 Apr 28;6:44. doi: 10.1186/1743-422X-6-44.

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

Author information

1
SIGA Technologies Inc, Corvallis, Oregon 97333, USA. ychen@siga.com

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.

PMID:
19400954
PMCID:
PMC2685784
DOI:
10.1186/1743-422X-6-44
[Indexed for MEDLINE]
Free PMC Article

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