Regions of the CD4 molecule not involved in virus binding or syncytia formation are required for HIV-1 infection of lymphocytes

J Immunol. 1992 Mar 15;148(6):1841-6.

Abstract

Cell surface-expressed CD4 binds to the envelope glycoprotein of HIV-1 and mediates syncytia formation through interacting with membrane expressed HIV-1 gp120. Further possible roles of the CD4 molecule in the process of cell infection by HIV-1 remain poorly understood. In our study we describe two mAb that recognize the V3/V4 domain of the CD4 molecule. Although these mAb do not inhibit gp120-CD4 binding or HIV-1-induced syncytia formation, they inhibit HIV-1 infection of human PBL. These findings suggest that discrete, definable domains of the CD4 molecule may be involved in interactions after HIV-1 envelope binding that lead to virus entry into the cell.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies, Monoclonal / immunology
  • Binding Sites
  • CD4 Antigens / immunology
  • CD4 Antigens / metabolism*
  • Calcium / metabolism
  • Cell Fusion*
  • Epitopes
  • HIV Envelope Protein gp120 / metabolism
  • HIV Infections / microbiology*
  • HIV-1 / metabolism*
  • Humans
  • Receptors, Antigen, T-Cell / physiology
  • Recombinant Proteins / metabolism
  • Signal Transduction
  • Solubility
  • T-Lymphocytes / microbiology*

Substances

  • Antibodies, Monoclonal
  • CD4 Antigens
  • Epitopes
  • HIV Envelope Protein gp120
  • Receptors, Antigen, T-Cell
  • Recombinant Proteins
  • Calcium