Varicella-zoster virus gH:gL contains a structure reactive with the anti-human gamma chain of IgG near the glycosylation site.
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.
Yokoyama
Tomonori
T
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.
Ayabe
Satoko
S
Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
Miyagi
Huminori
H
Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
Sugano
Toru
T
Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
Otsu
Akira
A
Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
Sato
Hitoshi
H
Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan1.
Kageyama
Seiji
S
Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan1.
Fujii
Takao
T
Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2.
Shiraki
Kimiyasu
K
Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan1.
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*
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