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Interaction of an anti-HIV peptide, T22, with gp120 and CD4.
Tamamura, H; Otaka, A; Murakami, T; Ishihara, T; Ibuka, T; Waki, M; Matsumoto, A; Yamamoto, N; Fujii, N.
Afiliación
  • Tamamura H; Faculty of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Japan.
Biochem Biophys Res Commun ; 219(2): 555-9, 1996 Feb 15.
Article en En | MEDLINE | ID: mdl-8605026
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.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Antivirales / Péptidos / Antígenos CD4 / Proteína gp120 de Envoltorio del VIH / VIH-1 / Péptidos Catiónicos Antimicrobianos Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 1996 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Antivirales / Péptidos / Antígenos CD4 / Proteína gp120 de Envoltorio del VIH / VIH-1 / Péptidos Catiónicos Antimicrobianos Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 1996 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos