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J. Virol. doi:10.1128/JVI.01971-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The Vaccinia Virus B5 Protein Requires A34 for Efficient Intracellular Trafficking from the ER to the Site of Wrapping and Incorporation into Progeny Virions

Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, New York 14642

^* To whom correspondence should be addressed. Email: Brian_Ward{at}urmc.rochester.edu.

	Abstract

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 B5R fused to the enhance green fluorescent protein (B5R-GFP) was created (vB5R-GFP/A34R) to investigate the role of A34 during virion morphogenesis. Cells infected with vB5R-GFP/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 demonstrate that B5-GFP localizes with the endoplasmic reticulum in the absence of A34. Expression of either the full-length A34 or a construct consisting of the lumenal and transmembrane domain restored normal trafficking of B5-GFP to the site of wrapping in the juxta-nuclear region. Co-immune precipitation studies confirmed that B5 and A34 interact through their lumenal domains and further analysis revealed that in the absence of A34, B5 is not efficiently incorporated into virions released from the cell.