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Interaction of an anti-HIV peptide, T22, with gp120 and CD4.

Authors :
Tamamura H
Otaka A
Murakami T
Ishihara T
Ibuka T
Waki M
Matsumoto A
Yamamoto N
Fujii N
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1996 Feb 15; Vol. 219 (2), pp. 555-9.
Publication Year :
1996

Abstract

T22 ([Tyr5,12, Lys7]-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.

Details

Language :
English
ISSN :
0006-291X
Volume :
219
Issue :
2
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
8605026
Full Text :
https://doi.org/10.1006/bbrc.1996.0272