Characteristics of a Neutralizing Monoclonal Antibody to the HIV Envelope Glycoprotein

M. A. Skinner, R. Ting, A. J. Langlois, K. J. Weinhold, H. K. Lyerly, K. Javaherian, T. J. Matthews

Research output: Contribution to journalArticlepeer-review

109 Scopus citations


We have studied the biologic and physical properties of a monoclonal antibody that binds to gp120, the exterior envelope glycoprotein of the human immunodeficiency virus (HIV) strain HTLV-IIIB. Designated 9284, the antibody possesses viral neutralizing activity and inhibits syncytium formation by infected cells. The antibody recognized a region of the polypeptide backbone previously described as an important neutralizing epitope. This region lies 307-330 residues from amino terminus of the glycoprotein. We have compared the biologic and physical properties of this antibody to those of the recently described 0.5β monoclonal antibody to gp120. The 0.5β antibody was biologically more potent and bound an epitope slightly downstream to that of the 9284 antibody. The antibodies did not differ significantly in their affinity for gp120. In competition studies, the o.5β antibody was displaced by the 9284 antibody, but the binding of the latter was unaffected by 0.5β.

Original languageEnglish (US)
Pages (from-to)187-197
Number of pages11
JournalAIDS research and human retroviruses
Issue number3
StatePublished - Jan 1 1988

ASJC Scopus subject areas

  • Immunology
  • Virology
  • Infectious Diseases


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