A Single gD Glycoprotein Can Mediate Infection by Herpes simplex Virus
Author(s) -
Richard W. Clarke,
Anna Drews,
Helena Browne,
David Klenerman
Publication year - 2013
Publication title -
journal of the american chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.115
H-Index - 612
eISSN - 1520-5126
pISSN - 0002-7863
DOI - 10.1021/ja4038406
Subject(s) - glycoprotein , herpes simplex virus , neutralization , chemistry , virology , monoclonal antibody , virus , antibody , viral entry , herpesvirus glycoprotein b , herpesviridae , viral disease , biochemistry , immunology , biology , viral replication
Herpes simplex viruses display hundreds of gD glycoproteins, and yet their neutralization requires tens of thousands of antibodies per virion, leading us to ask whether a wild-type virion with just a single free gD is still infective. By quantitative analysis of fluorescently labeled virus particles and virus neutralization assays, we show that entry of a wild-type HSV virion to a cell does indeed require just one or two of the approximately 300 gD glycoproteins to be left unbound by monoclonal antibody. This indicates that HSV entry is an extraordinarily efficient process, functioning at the level of single molecular complexes.
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