Membrane Proteins Specified by Herpes Simplex Viruses. III. Role of Glycoprotein VP7(B2) in Virion Infectivity

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1979 Mar 1

PMID 221669

Citations 165

Authors

M Sarmiento

M Haffey

P G Spear

Affiliations

Soon will be listed here.

Abstract

Experiments done with a temperature"sensitive mutant of herpes simplex virus type 1 (HSV-1) have revealed that one of the virisn glycoproteins, designated VP7(B2), is apparently not required for the production of enveloped virus particles, whereas it does play a critical role in virion infectivity. The mutant, designated HSV-1[HFEM]tsB5, fails to accumulate VP7(B2) at nonpermissive temperature and produces virions that lack detectable quantities of this glycoprotein and that have very low specific infectivity. The poor infectivity of the virions is most readily explained by failure of penetration into the host cell rather than by failure of adsorption to cells because it was shown that the VP7(B2)-deficient virions can bind to cells and that polyethylene glycol, an agent known to promote membrane fusion, can significantly enhance infectivity of the adsorbed virions.

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