Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies.

Journal article

We have probed the structures of monomeric and oligomeric gp120 glycoproteins from the LAI isolate of human immunodeficiency virus type 1 (HIV-1) with a panel of monoclonal antibodies (MAbs); most of these MAbs are directed against continuous epitopes. On native monomeric gp120, most of the first conserved (C1) domain is accessible to MAbs, although some regions of C1 are relatively inaccessible. All of the MAbs directed against the C2, C3, and C5 domains bind preferentially to denatured mono...

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Authors: Moore, J; Sattentau, Q; Wyatt, R; Sodroski, J

• Publication status: Published
• Journal: Journal of virology
• Volume: 68
• Issue: 1
• Pages: 469-484
• Publication date: 1994-01-01
• EISSN: 1098-5514
• ISSN: 0022-538X
• Language: English
• Keywords: Amino Acid Sequence; Epitopes; Molecular Sequence Data; Recombinant Proteins; Conserved Sequence; HIV Envelope Protein gp41; Protein Conformation; HIV Envelope Protein gp120; HIV-1; HIV Antibodies; Antibodies, Monoclonal; Protein Denaturation