Varicella-zoster virus gH:gL contains a structure reactive with the anti-human gamma chain of IgG near the glycosylation site

• Published in: Journal of general virology 2001-02, Vol.82 (2), p.331-334
• Main Authors: Yokoyama, Tomonori, Ayabe, Satoko, Miyagi, Huminori, Sugano, Toru, Otsu, Akira, Sato, Hitoshi, Kageyama, Seiji, Fujii, Takao, Shiraki, Kimiyasu
• Format: Article
• Language: English
• Subjects: Antibodies, Monoclonal - immunology; Biosensing Techniques; Concanavalin A - immunology; Enzyme-Linked Immunosorbent Assay; Glycoproteins - chemistry; Glycoproteins - immunology; Glycosylation; Herpesvirus 3, Human - chemistry; Herpesvirus 3, Human - immunology; Humans; Immunoglobulin G - chemistry; Immunoglobulin G - immunology; Immunoglobulin Heavy Chains - chemistry; Immunoglobulin Heavy Chains - immunology; Immunoglobulin kappa-Chains - chemistry; Immunoglobulin kappa-Chains - immunology; Immunoglobulin lambda-Chains - chemistry; Immunoglobulin lambda-Chains - immunology; Neutralization Tests; varicella-zoster virus; Viral Proteins - chemistry; Viral Proteins - immunology
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-82-2-331

Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan 1 Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan 2 Author for correspondence: Kimiyasu Shiraki. Fax [phone]. e-mail kshiraki{at}toyama-mpu.ac.jp Varicella-zoster virus (VZV) glycoproteins were purified from infected cells using monoclonal antibodies and gH:gL was found to react with antibodies to the 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 chain (anti-h- -IgG). gH:gL reacted with anti-h- -IgG in an ELISA assay and gave a K d value of 2·16 x 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 x 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- -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.