RT Journal Article SR Electronic(1) A1 Yokoyama, Tomonori A1 Ayabe, Satoko A1 Miyagi, Huminori A1 Sugano, Toru A1 Otsu, Akira A1 Sato, Hitoshi A1 Kageyama, Seiji A1 Fujii, Takao A1 Shiraki, KimiyasuYR 2001 T1 Varicella-zoster virus gH:gL contains a structure reactive with the anti-human gamma chain of IgG near the glycosylation site JF Journal of General Virology, VO 82 IS 2 SP 331 OP 334 DO https://doi.org/10.1099/0022-1317-82-2-331 PB Microbiology Society, SN 1465-2099, AB 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 K d value of 2·16×10−7 M in a BIAcore assay. The K d value of the human monoclonal antibody to gH (TI-57) used for the purification of gH:gL was 4·45×10−10 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-82-2-331