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Interaction of an anti-HIV peptide, T22, with gp120 and CD4.
- 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.
- Subjects :
- Amino Acid Sequence
Antiviral Agents pharmacology
Baculoviridae
Biosensing Techniques
CD4 Antigens drug effects
Cell Line
Humans
Kinetics
Membrane Fusion drug effects
Molecular Sequence Data
Peptides pharmacology
Protein Binding
Recombinant Proteins drug effects
Recombinant Proteins metabolism
Sequence Homology, Amino Acid
T-Lymphocytes immunology
T-Lymphocytes virology
Antimicrobial Cationic Peptides
Antiviral Agents metabolism
CD4 Antigens metabolism
HIV Envelope Protein gp120 metabolism
HIV-1 drug effects
Peptides metabolism
Subjects
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