title: Varicella-zoster virus gH:gL contains a structure reactive with the anti-human gamma chain of IgG near the glycosylation site.
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 gamma 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 gamma chain (anti-h-gamma-IgG). gH:gL reacted with anti-h-gamma-IgG in an ELISA assay and gave a K:(d) value of 2.16x10(-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 4.45x10(-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-gamma-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.
authors.affiliation: Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.|Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan1.
authors.forename: Tomonori
authors.initials: T
authors.lastname: Yokoyama
authors.affiliation: Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
authors.forename: Satoko
authors.initials: S
authors.lastname: Ayabe
authors.affiliation: Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
authors.forename: Huminori
authors.initials: H
authors.lastname: Miyagi
authors.affiliation: Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
authors.forename: Toru
authors.initials: T
authors.lastname: Sugano
authors.affiliation: Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
authors.forename: Akira
authors.initials: A
authors.lastname: Otsu
authors.affiliation: Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan1.
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Sato
authors.affiliation: Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan1.
authors.forename: Seiji
authors.initials: S
authors.lastname: Kageyama
authors.affiliation: Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
authors.forename: Takao
authors.initials: T
authors.lastname: Fujii
authors.affiliation: Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan1.
authors.forename: Kimiyasu
authors.initials: K
authors.lastname: Shiraki
mesh_terms: D000911:Antibodies, Monoclonal / Q000276:immunology; D015374:Biosensing Techniques; D003208:Concanavalin A / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay; D006023:Glycoproteins / Q000737:chemistry* / Q000276:immunology*; D006031:Glycosylation; D014645:Herpesvirus 3, Human / Q000737:chemistry* / Q000276:immunology*; D006801:Humans; D007074:Immunoglobulin G / Q000737:chemistry* / Q000276:immunology*; D007143:Immunoglobulin Heavy Chains / Q000737:chemistry / Q000276:immunology; D007145:Immunoglobulin kappa-Chains / Q000737:chemistry / Q000276:immunology; D007146:Immunoglobulin lambda-Chains / Q000737:chemistry / Q000276:immunology; D009500:Neutralization Tests; D014764:Viral Proteins / Q000737:chemistry / Q000276:immunology*
chemical_list: D000911:Antibodies, Monoclonal; D006023:Glycoproteins; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains; D007145:Immunoglobulin kappa-Chains; D007146:Immunoglobulin lambda-Chains; D014764:Viral Proteins; D003208:Concanavalin A