Abstract
The site on HIV-1 gp120 that binds to the CD4 receptor is vulnerable to antibodies. However, most antibodies that interact with this site cannot neutralize HIV-1. To understand the basis of this resistance, we determined co-crystal structures for two poorly neutralizing, CD4-binding site (CD4BS) antibodies, F105 and b13, in complexes with gp120. Both antibodies exhibited approach angles to gp120 similar to those of CD4 and a rare, broadly neutralizing CD4BS antibody, b12. Slight differences in recognition, however, resulted in substantial differences in F105- and b13-bound conformations relative to b12-bound gp120. Modeling and binding experiments revealed these conformations to be poorly compatible with the viral spike. This incompatibility, the consequence of slight differences in CD4BS recognition, renders HIV-1 resistant to all but the most accurately targeted antibodies.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, N.I.H., Intramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Antibodies, Neutralizing / chemistry
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Antibodies, Neutralizing / immunology*
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Antibodies, Neutralizing / metabolism
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Binding Sites
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Binding Sites, Antibody
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CD4 Antigens / chemistry
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CD4 Antigens / metabolism*
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Crystallography, X-Ray
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Epitopes
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HIV Antibodies / chemistry*
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HIV Antibodies / immunology*
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HIV Antibodies / metabolism
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HIV Envelope Protein gp120 / chemistry*
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HIV Envelope Protein gp120 / immunology*
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HIV Envelope Protein gp120 / metabolism
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HIV-1
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Humans
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Hydrophobic and Hydrophilic Interactions
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Immune Evasion*
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / immunology
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Peptide Fragments / metabolism
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Protein Conformation
Substances
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Antibodies, Neutralizing
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CD4 Antigens
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Epitopes
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HIV Antibodies
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HIV Envelope Protein gp120
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HIV envelope protein gp120 (305-321)
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Peptide Fragments
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gp120 protein, Human immunodeficiency virus 1
Associated data
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PDB/3HI1
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PDB/3IDX
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PDB/3IDY