Interaction of an anti-HIV peptide, T22, with GP120 and CD4

被引:28
|
作者
Tamamura, H
Otaka, A
Murakami, T
Ishihara, T
Ibuka, T
Waki, M
Matsumoto, A
Yamamoto, N
Fujii, N
机构
[1] KYOTO UNIV,FAC PHARMACEUT SCI,SAKYO KU,KYOTO 606,JAPAN
[2] TOKYO MED & DENT UNIV,SCH MED,BUNKYO KU,TOKYO 113,JAPAN
[3] SEIKAGAKU CORP,CHUO KU,TOKYO 103,JAPAN
关键词
D O I
10.1006/bbrc.1996.0272
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
T22 ([Tyr(5,12), Lys(7)]-polyphemusin II) has been shown to have strong anti-human immunodeficiency virus (HIV) activity. The precise mechanism of action of T22 on HIV-replication has not been elucidated yet, nor have the targets of T22 been identified. However, our previous research suggested that T22 exerts its effect by blocking virus-cell fusion and that T22 might interact with an HIV envelope protein and/or a T-cell surface protein. Herein we use a novel biosensor based on the principles of surface plasmon resonance (BIAcore) to demonstrate that T22 binds specifically to both gp120 (an envelope protein of HIV) and CD4 (a T-cell surface protein) and that both bindings can be inhibited by an anti-T22 antibody. The data obtained suggest that T22 inhibits virus-cell fusion through the double binding to the above two proteins. (C) 1996 Academic Press, inc.
引用
收藏
页码:555 / 559
页数:5
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