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Journal of General Virology (2001), 82, 331-334.
© 2001 Society for General Microbiology

Animal: DNA Viruses

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

Tomonori Yokoyama1,2, Satoko Ayabe2, Huminori Miyagi2, Toru Sugano2, Akira Otsu2, Hitoshi Sato1, Seiji Kageyama1, Takao Fujii2 and Kimiyasu Shiraki1

Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan1
Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan2

Author for correspondence: Kimiyasu Shiraki. Fax +81 76 434 5020. 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 {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 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-{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.




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T. J. Pasieka, L. Maresova, K. Shiraki, and C. Grose
Regulation of Varicella-Zoster Virus-Induced Cell-to-Cell Fusion by the Endocytosis-Competent Glycoproteins gH and gE
J. Virol., March 15, 2004; 78(6): 2884 - 2896.
[Abstract] [Full Text] [PDF]


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