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

Biochemical and Biophysical Research Communications
H TamamuraN Fujii

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.

Citations

Jul 19, 2006·Clinical Microbiology Reviews·Håvard JenssenRobert E W Hancock
May 20, 1999·Biopolymers·D Andreu, L Rivas
Apr 25, 2008·Current Protocols in Immunology·David Andreu, Paula Gomes
Apr 21, 2012·Organic & Biomolecular Chemistry·Shinya Oishi, Nobutaka Fujii
May 3, 2013·Probiotics and Antimicrobial Proteins·Nicolás I TorresMichael L Chikindas
Aug 22, 2020·Biomaterials Science·Thomas J HallSophie C Cox
Apr 23, 2003·The Journal of Immunology : Official Journal of the American Association of Immunologists·Wei WangRobert I Lehrer

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