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Molecular ans stractural basis of beta-barrel membrane pore-forming proteins for design of cell-specific nanotools.

Research Project

Project/Area Number 16K14897
Research Category

Grant-in-Aid for Challenging Exploratory Research

Allocation TypeMulti-year Fund
Research Field Applied biochemistry
Research InstitutionTohoku University

Principal Investigator

Kaneko Jun  東北大学, 農学研究科, 准教授 (30221188)

Project Period (FY) 2016-04-01 – 2018-03-31
Project Status Completed (Fiscal Year 2017)
Budget Amount *help
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2017: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2016: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
Keywordsβ-PFTs / 膜孔形成機構 / Staphylococcus / beta-pore forming toxin / cell specificity / pore forming mechanism / タンパク質工学 / βバレル形成機能 / ナノツール
Outline of Final Research Achievements

Molecular mechanism of beta-barrel membrane pore-forming toxin of Staphylococcus aureus was investigated.
In target cell specificity, loop 4 of Hlg2 and LukE rim domain, which contacts with host cell surface, was essential to binding to human erythrocytes, and loop1 and 2 were found to be assisting the binding. We also found that the interaction between Asp in the cap region involved in the prestem retention in LukF and basic amino acids in the adjacent Hlg2 cap site by membrane pore formation involved in the prestem release of γ-hemolysin. Furthermore, double cysteine mutant of α-hemolysin capable of regulating the release of prestem was constructed. Using this system, now the residues involved in the stem insertion are being analyzed.

Report

(3 results)
  • 2017 Annual Research Report   Final Research Report ( PDF )
  • 2016 Research-status Report
  • Research Products

    (6 results)

All 2018 2017 2016

All Journal Article (1 results) (of which Peer Reviewed: 1 results) Presentation (5 results) (of which Invited: 1 results)

  • [Journal Article] Rim domain loops of Staphylococcal β-pore forming bi-component toxin S-components recognize target human erythrocytes in a coordinated manner.2018

    • Author(s)
      Peng Z, Takeshita M, Shibata N, Tada H, Tanaka Y, Kaneko J.
    • Journal Title

      J. Biochem.

      Volume: 印刷中(電子版発行済) Issue: 2 Pages: 93-102

    • DOI

      10.1093/jb/mvy030

    • NAID

      40021635138

    • Related Report
      2017 Annual Research Report
    • Peer Reviewed
  • [Presentation] Intermolecular switch for stem release in the staphylococcal bi-component toxin g-hemolysin for b-barrel pore assembly2018

    • Author(s)
      Kein TAKEDA, Yoshikazu TANAKA, Jun KANEKO
    • Organizer
      日本農芸化学会2018年大会
    • Related Report
      2017 Annual Research Report
  • [Presentation] 黄色ブドウ球菌の二成分性毒素LukEDにおけるS型成分の細胞特異性に関わる領域の解析2017

    • Author(s)
      彭 昭、金子 淳
    • Organizer
      第90回日本細菌学会総会
    • Place of Presentation
      仙台国際センター(宮城県・仙台市)
    • Year and Date
      2017-03-19
    • Related Report
      2016 Research-status Report
  • [Presentation] Analysis of the regions involved in the cell specificity of the S-component of staphylococcal bi-component toxin LukED2017

    • Author(s)
      Zhao PENG and Jun KANEKO
    • Organizer
      第90回日本細菌学会総会
    • Related Report
      2017 Annual Research Report
  • [Presentation] 黄色ブドウ球菌における二成分性毒素γヘモリジンの膜孔形成機構の解明2017

    • Author(s)
      武田慶胤、田中良和、金子淳
    • Organizer
      第62回ブドウ球菌研究会
    • Related Report
      2017 Annual Research Report
  • [Presentation] 黄色ブドウ球菌のβバレル膜孔形成毒素の膜孔形成及び遺伝子の伝播機構2016

    • Author(s)
      金子 淳、田中 良和
    • Organizer
      第63回トキシンシンポジウム
    • Place of Presentation
      ほほえみの宿 滝の湯(山形県・天童市)
    • Year and Date
      2016-07-14
    • Related Report
      2016 Research-status Report
    • Invited

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Published: 2016-04-21   Modified: 2019-03-29  

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