Interaction of an anti-HIV peptide, T22, with gp120 and CD4.
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.
Tamamura
H
H
Faculty of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Japan.
Otaka
A
A
Murakami
T
T
Ishihara
T
T
Ibuka
T
T
Waki
M
M
Matsumoto
A
A
Yamamoto
N
N
Fujii
N
N
D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides; D000998:Antiviral Agents / Q000378:metabolism* / Q000494:pharmacology; D016367:Baculoviridae; D015374:Biosensing Techniques; D015704:CD4 Antigens / Q000187:drug effects / Q000378:metabolism*; D002460:Cell Line; D015699:HIV Envelope Protein gp120 / Q000378:metabolism*; D015497:HIV-1 / Q000187:drug effects*; D006801:Humans; D007700:Kinetics; D008561:Membrane Fusion / Q000187:drug effects; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D011994:Recombinant Proteins / Q000187:drug effects / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013601:T-Lymphocytes / Q000276:immunology / Q000821:virology
D023181:Antimicrobial Cationic Peptides; D000998:Antiviral Agents; D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120; D010455:Peptides; D011994:Recombinant Proteins; C076963:T22 protein, synthetic