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Elucidation of HIV-1 envelope incorporation into virions

Research Project

Project/Area Number 14570268
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Virology
Research InstitutionUniversity of the Ryukyus

Principal Investigator

MURAKAMI Tsutomu  University of the Ryukyus, Graduate School of Medicine, Associate Professor, 医学部, 助教授 (50336385)

Co-Investigator(Kenkyū-buntansha) YOSHIDA Atsushi  University of the Ryukyus, Graduate School of Medicine, Assistant Professor, 医学部, 助手 (10242778)
TANAKA Yuetsu  University of the Ryukyus, Graduate School of Medicine, Professor, 医学部, 教授 (30163588)
Project Period (FY) 2002 – 2003
Project Status Completed (Fiscal Year 2003)
Budget Amount *help
¥2,900,000 (Direct Cost: ¥2,900,000)
Fiscal Year 2003: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 2002: ¥1,700,000 (Direct Cost: ¥1,700,000)
KeywordsHIV-1 / Env proteins / Gag proteins / Virus binding / entry / Membrane fusion / Processing / Viral protease / プロテアーゼ
Research Abstract

We and others have presented evidence for a direct interaction between the matrix(MA) domain of the human immunodeficiency virus type 1(HIV-1) Gag protein and the cytoplasmic tail of the transmembrane envelope(Env) glycoprotein gp41. In addition, it has been postulated that the MA domain of Gag undergoes a conformational change following Gag processing and the cytoplasmic tail of gp41 has been shown to modulate Env-mediated membrane fusion activity. Together, these results raise the possibility that the interaction between the gp41 cytoplasmic tail and MA is regulated by protease(PR)-mediated Gag processing, perhaps affecting Env function. To examine whether Gag processing affects Env-mediated fusion, we compared the ability of WT HIV-1 Env and a mutant lacking the gp41 cytoplasmic tail to induce fusion in the context of an active(PR^+) or inactive(PR^-) viral PR. We observed that PR^-virions bearing WT Env displayed defects in cell-cell fusion. Impaired fusion did not pear to be due to differences in the levels of virion-associated Env, in CD4-dependent binding to target cells, or in the formation of the CD4-induced gp41 six-helix bundle. Interestingly, truncation of the gp41 cytoplasmic tail reversed the fusion defect. These results suggest that interactions between unprocessed Gag and the gp41 cytoplasmic tail suppress fusion.

Report

(3 results)
  • 2003 Annual Research Report   Final Research Report Summary
  • 2002 Annual Research Report
  • Research Products

    (5 results)

All Other

All Publications (5 results)

  • [Publications] Murakami, S., Ablan, EO., Y.Tanaka: "Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity"Journal of Virology. Vol.78,No.2. 1026-1031 (2004)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] 村上努, 田中勇悦, 山本直樹: "ウイルス・細菌と感染症がわかる:分担執筆HIVの感染機構と抗HIV薬開発の現状"羊土社. 133 (2004)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] Murakami, T., S.Ablan, E.O.Freed, Y.Tanaka.: "Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity."Journal of Virology.. Vol.78, No.2. 1026-1031 (2004)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] T.Murakami, S.Ablan, E.O.Freed, Y.Yanaka.: "Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity"Journal of Virology. Vol.78,No.2. 1026-1031 (2004)

    • Related Report
      2003 Annual Research Report
  • [Publications] 村上 努, 田中勇悦, 山本直樹: "ウイルス・細菌と感染症がわかる:分担執筆HIVの感染機構と抗HIV薬開発の現状"羊土社. 133 (2004)

    • Related Report
      2003 Annual Research Report

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Published: 2002-04-01   Modified: 2016-04-21  

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