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Published online ahead of print on 4 March 2009 as doi:10.1099/vir.0.009092-0
Journal of General Virology 2009;90:1582.

A more recent version of this article appeared on July 1, 2009 J Gen Virol (2009), DOI 10.1099/vir.0.009092-0
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Acidic residues in the membrane-proximal stalk region of vaccinia virus protein B5 are required for glycosaminoglycan-mediated disruption of the extracellular enveloped virus outer membrane

Kim L. Roberts1, Adrien Breiman1, Gemma Carter2, Helen Ewles1, Michael Hollinshead1, Mansun Law3 and Geoffrey L. Smith1,4

1 Imperial College London;
2 University of Oxford;
3 Scripps research Institute

4 E-mail: geoffrey.l.smith{at}imperial.ac.uk

The extracellular enveloped virus (EEV) form of vaccinia virus is surrounded by two lipid envelopes. This presents a topological problem for virus entry into cells because a classical fusion event would only release a virion surrounded by a single envelope into the cell. Recently, we described a mechanism in which the EEV outer membrane is disrupted following interaction with glycosaminoglycans (GAGs) on the cell surface and thus allowing fusion of the inner membrane with the plasma membrane and penetration of a naked core inside the cytosol. Here we show that both the B5 and A34 viral glycoproteins are required for this process. A34 is required to recruit B5 into the EEV membrane and B5 acts as a molecular switch to control EEV membrane rupture upon exposure to GAGs. Analysis of VACV strains expressing mutated B5 proteins demonstrated that the acidic stalk region between the transmembrane anchor sequence and the fourth short consensus repeat of B5 are critical for GAG-induced membrane rupture. Further, the interaction between B5 and A34 can be disrupted by the addition of polyanions (GAGs) and polycations but only the former induce membrane rupture. Based on these data we propose a revised model for the EEV entry.

Received 25 November 2008; accepted 23 February 2009.




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