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アンラク ケンサク
Kensaku Anraku
安楽 健作 所属 熊本保健科学大学 保健科学部 医学検査学科 熊本保健科学大学大学院 保健科学研究科 保健科学専攻 職位 教授 |
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| 発表年月日 | 2019/05/21 |
| 発表テーマ | DESIGN AND SYNTHESIS OF PHOSPHOLIPID DERIVATIVES EXHIBITING HIGH-AFFINITY BINDING FOR THE HIV-1 MA DOMAIN |
| 会議名 | Retroviruses |
| 主催者 | Cold Spring Harbor Laboratory |
| 学会区分 | 国際学会 |
| 発表形式 | ポスター |
| 単独共同区分 | 共同 |
| 開催地名 | Cold Spring Harbor, USA |
| 発表者・共同発表者 | Kensaku Anraku, Hiroshi Tateishi, Kazuaki Monde, Ryota Fukuda, Ryoko Koga, Kotaro Koiwai, Fumiaki Yumoto, Toshiya Senda, Shogo Misumi, Masami Otsuka, and Mikako Fujita |
| 概要 | The viral protein Pr55Gag is one of the products produced by hijacked host cells and mediates HIV-1 virion budding. As Pr55Gag-PIP2 binding triggers the virion budding, we considered that a small molecule that binds firmly to Pr55Gag could antagonize PIP2 in the Pr55Gag binding. We synthesized an artificial phosphoinositide, L-HIPPO (L-Heptanoylphosphatidyl Inositol Pentakisphosphate). L-HIPPO-α-CDE (cyclodextrin-dendridimer conjugate) complex suppressed membrane localization of Pr55Gag and subsequent virus release and induced apoptosis of the host cell.
In development of L-HIPPO, we also found that one of host cell’s phospholipid, cardiolipin (CL) binds to MA domain stronger than PIP2, and CL inhibited HIV-1 infectivity at low concentration. We designed and synthesized of CL derivatives, and these derivatives bound to MA domain with relative high affinity. |