Remodeling of Dynamic Structures of HIV Envelope Proteins and Chemical Synthesis of Artificial Antigen Molecules Inducing Neutralizing Antibodies

DOI
  • Nomura Wataru
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University
  • Nakahara Toru
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University
  • Hashimoto Chie
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University
  • Ohba kenji
    Yong Loo Lin School of Medicine, National University of Singapore
  • Soma Akira
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University
  • Tanaka Tomohiro
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University
  • Narumi Tetsuo
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University
  • Yamamoto Naoki
    Yong Loo Lin School of Medicine, National University of Singapore
  • Tamamura Hirokazu
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University

Bibliographic Information

Other Title
  • HIV侵入の動的超分子機構を模倣した立体構造特異的人工抗原分子の創製

Description

The membrane-fusion mechanism involved during entry into the cell of HIV-1 is mediated by envelope proteins (gp120/gp41) and receptors on the target cells (CD4/CCR5/CXCR4). A novel equivalently branched template with C3-symmetric linkers was designed and synthesized. Our synthetic antigen mimicking the N36 trimeric form was synthesized using this template. The antiserum produced by immunization of the N36 trimeric form antigen showed structural preference in binding to the N36 trimer. Furthermore, it was revealed that the antiserum has stronger inhibitory activity against HIV-1 infection than that induced by the N36 monomer. The present results suggest HIV vaccine design based on relationships to the natural structures of proteins involved in HIV fusion mechanisms is highly effective.

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Keywords

Details 詳細情報について

  • CRID
    1390282680611600768
  • NII Article ID
    130006997361
  • DOI
    10.14895/hannou.36.0.164.0
  • Text Lang
    ja
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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