Varicella-zoster virus gH:gL contains a structure reactive with the anti-human gamma chain of IgG near the glycosylation site
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 +81 76 434 5020. e-mail kshiraki{at}toyama-mpu.ac.jp Varic...
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Published in | Journal of general virology Vol. 82; no. 2; pp. 331 - 334 |
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Soc General Microbiol
01.02.2001
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Abstract | 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 +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 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. |
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AbstractList | 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. 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 sub(d) value of 2 super(.)16x10 super(-7)M in a BIAcore assay. The K sub(d) value of the human monoclonal antibody to gH (TI-57) used for the purification of gH:gL was 4 super(.)45x10 super(-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. 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. 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 +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 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. |
Author | Sugano, Toru Fujii, Takao Ayabe, Satoko Otsu, Akira Shiraki, Kimiyasu Sato, Hitoshi Yokoyama, Tomonori Kageyama, Seiji Miyagi, Huminori |
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Cites_doi | 10.1086/315336 10.1128/JVI.66.1.341-348.1992 10.1016/0042-6822(83)90175-7 10.1128/JVI.63.8.3435-3443.1989 10.1006/viro.1994.1007 10.1146/annurev.mi.44.100190.000423 10.1016/0042-6822(86)90124-8 10.1002/eji.1830170309 10.1099/0022-1317-61-2-255 10.1006/viro.1995.1359 10.1099/0022-1317-61-2-271 10.1099/0022-1317-72-9-2065 10.1016/S0264-410X(98)00035-8 10.1006/viro.1994.1145 10.1007/s007050050243 |
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References_xml | – volume: 181 start-page: 1158 year: 2000 ident: R6 article-title: Novel immunogenicity of Oka varicella vaccine vector expressing hepatitis B surface antigen publication-title: Journal of Infectious Diseases doi: 10.1086/315336 contributor: fullname: Kamiyama – volume: 66 start-page: 341 year: 1992 ident: R3 article-title: Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted publication-title: Journal of Virology doi: 10.1128/JVI.66.1.341-348.1992 contributor: fullname: Forrester – volume: 129 start-page: 357 year: 1983 ident: R9 article-title: Synthesis and processing of glycoproteins of varicella-zoster virus (VZV) as studied with monoclonal antibodies to VZV antigens publication-title: Virology doi: 10.1016/0042-6822(83)90175-7 contributor: fullname: Okuno – volume: 63 start-page: 3435 year: 1989 ident: R4 article-title: Neutralizing antibodies specific for glycoprotein H of herpes simplex virus permit viral attachment to cells but prevent penetration publication-title: Journal of Virology doi: 10.1128/JVI.63.8.3435-3443.1989 contributor: fullname: Fuller – volume: 198 start-page: 50 year: 1994 ident: R7 article-title: Functional roles of terminal glycomoieties in varicella-zoster virus infection publication-title: Virology doi: 10.1006/viro.1994.1007 contributor: fullname: Matsui – volume: 44 start-page: 59 year: 1990 ident: R5 article-title: Glycoproteins encoded by varicella-zoster virus: biosynthesis, phosphorylation, and intracellular trafficking publication-title: Annual Review of Microbiology doi: 10.1146/annurev.mi.44.100190.000423 contributor: fullname: Grose – volume: 149 start-page: 230 year: 1986 ident: R8 article-title: Neutralization of epitope of varicella-zoster virus on native viral glycoproteins gp118 (VZV glycoprotein gpIII) publication-title: Virology doi: 10.1016/0042-6822(86)90124-8 contributor: fullname: Montalvo – volume: 17 start-page: 359 year: 1987 ident: R14 article-title: Hybridomas producing human monoclonal antibodies against varicella-zoster virus publication-title: European Journal of Immunology doi: 10.1002/eji.1830170309 contributor: fullname: Sugano – volume: 61 start-page: 255 year: 1982 ident: R12 article-title: Polypeptides of varicella-zoster virus (VZV) and immunological relationship of VZV and herpes simplex virus (HSV) publication-title: Journal of General Virology doi: 10.1099/0022-1317-61-2-255 contributor: fullname: Shiraki – volume: 210 start-page: 429 year: 1995 ident: R1 article-title: Cell surface expression and fusion by the varicella-zoster virus gH: gL glycoprotein complex: analysis by laser scanning confocal microscopy publication-title: Virology doi: 10.1006/viro.1995.1359 contributor: fullname: Duus – volume: 61 start-page: 271 year: 1982 ident: R11 article-title: Virus particles and glycoproteins excreted from cultured cells infected with varicella-zoster virus (VZV) publication-title: Journal of General Virology doi: 10.1099/0022-1317-61-2-271 contributor: fullname: Shiraki – volume: 72 start-page: 2065 year: 1991 ident: R15 article-title: A human monoclonal antibody against varicella-zoster virus glycoprotein III publication-title: Journal of General Virology doi: 10.1099/0022-1317-72-9-2065 contributor: fullname: Sugano – volume: 16 start-page: 1263 year: 1998 ident: R10 article-title: Immune response to varicella-zoster virus glycoproteins in guinea pigs infected with Oka varicella vaccine publication-title: Vaccine doi: 10.1016/S0264-410X(98)00035-8 contributor: fullname: Sato – volume: 199 start-page: 458 year: 1994 ident: R2 article-title: Neutralization epitope of the varicella-zoster virus gH: gL glycoprotein publication-title: Virology doi: 10.1006/viro.1994.1145 contributor: fullname: Forghani – volume: 142 start-page: 2295 year: 1997 ident: R13 article-title: Functions of purified gB, gE: gl, and gH:gL, and their sialyl residues in varicella-zoster virus infection publication-title: Archives of Virology doi: 10.1007/s007050050243 contributor: fullname: Shiraki |
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Teijin Institute for Biomedical Research,... Varicella-zoster virus (VZV) glycoproteins were purified from infected cells using monoclonal antibodies and gH:gL was found to react with antibodies to the... 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... |
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SubjectTerms | 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 |
Title | Varicella-zoster virus gH:gL contains a structure reactive with the anti-human gamma chain of IgG near the glycosylation site |
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