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The role of glycosylation in determining the immunogenicity of influenza C virus glycoprotein

Research Project

Project/Area Number 60480169
Research Category

Grant-in-Aid for General Scientific Research (B)

Allocation TypeSingle-year Grants
Research Field Virology
Research InstitutionYamagata University

Principal Investigator

NAKAMURA Kiyoto  Yamagata University School of Medicine Professor, 医学部, 教授 (00125775)

Co-Investigator(Kenkyū-buntansha) SUGAWARA Kanetsu  Yamagata University School of Medicine Staff for Education and Research, 医学部, 教務職員 (60110673)
NISHIMURA Hidekazu  Yamagata University School of Medicine Assistant, 医学部, 助手 (50172698)
KITAME Fumio  Yamagata University School of Medicine Associate Professor, 医学部, 助教授 (40004676)
Project Period (FY) 1985 – 1986
Project Status Completed (Fiscal Year 1986)
Budget Amount *help
¥6,800,000 (Direct Cost: ¥6,800,000)
Fiscal Year 1986: ¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 1985: ¥3,500,000 (Direct Cost: ¥3,500,000)
KeywordsInfluenza C Virus / Glycoprotein / Carbohydratos / Immunogenicity / モノクローナル抗体
Research Abstract

The aim of this study is to understand the role of glycosylation in determining the immunogenicity of influenza C virus glycoprotein, gp88. To this goal, the antigenicity of gp88 was compared with its nonglycosylated form (T76) synthesized in the presence of tunicamycin, utilizing seven monoclonal antibodies raised against gp88 of the C/Ann Arbor/1/50 strain. These monoclonal antibodies could be classified into two groups, A and B. Group A inhibits hemagglutination, hemolysis and infectivity of the virus whereas group B does not. Radioimmunoprecipitation experiments revealed that three antibodies in group B were all reactive with T76 as well as with gp88. In contrast, three out of four antibodies in group A did not precipitate T76 at all, and only a limited amount of the polypeptide was precipitated with the other antibody of this group. Western blot analysis also showed that denatured gp88 blotted on nitrocellulose was reactive with group B antibodies but not with group A. From these observations, we conclude that glycosylation of gp88 selectively influences the integrity of biologically active and conformation-dependent epitopes recognized by group A antibodies. It is reasonable to assume, therefore, that in the absence of glycosylation, the gp88 glycoprotein may fail to attain an appropriate conformation, and as a result, may be unable to elicit neutralizing antibodies.

Report

(1 results)
  • 1986 Final Research Report Summary
  • Research Products

    (11 results)

All Other

All Publications (11 results)

  • [Publications] 中村喜代人,本郷誠治,菅原勘悦: 臨床病理. 33. 122-128 (1985)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Hongo,S.;Sugawara,K.;Homma,M.;Nakamura,K.: Vaccine. 3. 223-226 (1985)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Hongo,S.;Sugawara,K.;Homma,M.;Nakamura,K.: Archives of Virology. 89. 171-187 (1986)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Hongo,S.;Sugawara,K.;Homma,M;Nakamura,K.: Archives of Virology. 89. 189-201 (1986)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Sugawara,K.;Nishimura,H.;Kitame,F.;Nakamura,K.: Virus Research. 6. 27-32 (1986)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Sugawara,K.;Nishimura,H.;Kitame,F.;Nakamura,K.: Virus Research. (1987)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Hongo,S.; Sugawara, K.; Homma, M.; Nakamura, K.: "Effects of glycosylation on the conformation and antigenicity of influenza C viral glycoproteins" Vaccine. 3. 223-226 (1985)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Hongo, S.; Sugawara, K.; Homma, M.; Nakamura, K.: "The functions of oligosaccharide chains associated with influenza C viral glycoproteins. <I> . The formation of influenza C virus particles in the absence of glycosylation." Arch. Virol.89. 171-187 (1986)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Hongo, S.; Sugawara, K.; Homma, M.; Nakamura, K.: "The functions of oligosaccharide chains associated with influenza C viral glycoproteins. <II> . The role of carbohydrates in the antigenic properties of influenza C viral glycoproteins." Arch. Virol.89. 189-201 (1986)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Sugawara, K.; Nishimura, H.; Kitame, F.; Nakamura, K.: "Antigenic variation among human strains of influenza C virus detected with monoclonal antibodies to gp88 glycoprotein." Virus Res.6. 27-32 (1986)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Sugawara, K.; Nishimura, H.; Kitame, F.; Nakamura, K.: "Glycosylation-dependent epitopes of influenza C virus glycoprotein." Virus Res. submitted.

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary

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Published: 1987-03-31   Modified: 2016-04-21  

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