Abstract
Varicella-zoster virus (VZV) glycoproteins were purified from infected cells using monoclonal antibodies and gH:gL was found to react with antibodies to the γ chain of human IgG (h-IgG), whereas gE:gI and gB did not. When gH:gL was captured by concanavalin A, it lost reactivity with the anti-h-IgG γ chain (anti-h-γ-IgG). gH:gL reacted with anti-h-γ-IgG in an ELISA assay and gave a Kd value of 2·16x10-7 M in a BIAcore assay. The Kd value of the human monoclonal antibody to gH (TI-57) used for the purification of gH:gL was 4·45x10-10 M. Virus pretreated with anti-h-IgG was five times more resistant to neutralization with TI-57. Although the nature of the binding was not clear, gH:gL bound to anti-h-γ-IgG. If this interaction results from immunological similarity between gH:gL and h-IgG, it may cause immune evasion in the pathogenesis of VZV infection.