Abstract
The attachment of human immunodeficiency virus type 1 (HIV-1) to target cells is mediated by a specific interaction between the viral envelope glycoprotein (gp120) and the CD4 receptor. Here we report that approximately 10% of HIV-1-infected individuals produce antibodies that recognize the extracellular portion of the CD4 molecule. Carboxyl-terminal deletions of CD4 that do not affect HIV-1 gp120 binding eliminate recognition of CD4 by patient antisera. In contrast, mutations in the amino-terminal domain of CD4 that attenuate HIV-1 gp120 binding do not diminish CD4 recognition by patient antisera. These results suggest that HIV-1 infection can generate antibodies directed against a region of the viral receptor distinct from the virus-binding domain.
Publication types
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Comparative Study
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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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Acquired Immunodeficiency Syndrome / immunology*
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Amino Acid Sequence
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Antigens, Surface
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Autoantibodies / analysis*
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Binding Sites
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Codon
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DNA / genetics
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HIV Envelope Protein gp120
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HIV Seropositivity
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HIV-1*
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Humans
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Immunosorbent Techniques
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Molecular Sequence Data
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Mutation
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Plasmids
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Receptors, HIV
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Receptors, Virus / genetics
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Receptors, Virus / immunology*
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Receptors, Virus / metabolism
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Recombinant Proteins
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Retroviridae Proteins / metabolism
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Transfection
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Viral Envelope Proteins
Substances
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Antigens, Surface
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Autoantibodies
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Codon
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HIV Envelope Protein gp120
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Receptors, HIV
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Receptors, Virus
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Recombinant Proteins
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Retroviridae Proteins
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Viral Envelope Proteins
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DNA