Abstract
The binding of a panel of monoclonal antibodies to V1, V2, and V3 loop-deleted HIV-1 gp120 was studied by competition analysis. Most of the previously defined relationships between gp120 epitopes were preserved on the variable loop-deleted protein, although interactions between some epitopes were dependent on the presence of the V1, V2, and V3 loops. Enzymatic deglycosylation of the variable loop-deleted protein only minimally altered the binding of most antibodies examined. Thus, a carbohydrate-deficient, conserved HIV-1 gp120 core can be produced that has a structure closely approximating that of the full-length, correctly folded gp120 monomer.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Antibodies, Monoclonal / immunology*
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Antigen-Antibody Reactions
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Antigenic Variation
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Binding Sites, Antibody
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Binding, Competitive
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CD4 Antigens / immunology
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Enzyme-Linked Immunosorbent Assay
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Epitopes / immunology
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Glycoside Hydrolases
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Glycosylation
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HIV Antibodies / immunology*
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HIV Envelope Protein gp120 / chemistry*
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HIV Envelope Protein gp120 / immunology*
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HIV-1 / immunology*
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Humans
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Molecular Sequence Data
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Structure-Activity Relationship
Substances
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Antibodies, Monoclonal
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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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Glycoside Hydrolases