Journal
JOURNAL OF VIROLOGY
Volume 82, Issue 5, Pages 2161-2169Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01971-07
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Funding
- NIAID NIH HHS [AI067391, K22 AI054392, R01 AI067391, AI54392] Funding Source: Medline
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The glycoproteins encoded by the vaccinia virus A34R and B5R genes are involved in intracellular envelope virus formation and are highly conserved among orthopoxviruses. A recombinant virus that has the A34R gene deleted and the B5R gene replaced with a B5R gene fused to the enhanced green fluorescent protein (B5R-GFP) gene was created (vB5RrGFP/Delta A34R) to investigate the role of A34 during virion morphogenesis. Cells infected with vB5R-GFP/Delta A34R displayed GFP fluorescence throughout the cytoplasm, which differed markedly from that seen in cells infected with a normal B5R-GFP-expressing virus (vB5R-GFP). Immunofluorescence and subcellular fractionation demonstrated that B5-GFP localizes with the endoplasmic reticulum in the absence of A34. Expression of either full-length A34 or a construct consisting of the lumenal and transmembrane domains restored normal trafficking of B5-GFP to the site of wrapping in the juxtanuclear region. Coimmunoprecipitation studies confirmed that B5 and A34 interact through their luminal domains, and further analysis revealed that in the absence of A34, B5 is not efficiently incorporated into virions released from the cell.
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