Characterization of a putative cellular receptor for HIV-1 transmembrane glycoprotein using synthetic peptides

AIDS. 1990 Jun;4(6):553-8. doi: 10.1097/00002030-199006000-00009.

Abstract

The transmembrane glycoprotein (gp41 or TM) of HIV-1 contains limited sequence similarity to TM of some immunosuppressive animal retroviruses. A specific HIV-1 TM sequence, denoted CS3, inhibits T-cell activation in vitro and antibody specific to CS3 has been linked to the absence of disease. CS3, when conjugated to human serum albumin (HSA) and labeled with fluorescein, binds specifically to CD4+ cell lines. Cross-linking of CS3-HSA to its binding activity on the CD4+ cell line RH9 reveals a putative subunit size of approximately 44 kD. Incubation of RH9 cells with CS3-HSA prior to addition of HIV-1 prevented HIV-1-mediated cell lysis and inhibited infection. These results suggest that the CS3 region of TM plays an important role in the pathogenesis of the AIDS virus, HIV-1.

Publication types

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

MeSH terms

  • Acquired Immunodeficiency Syndrome / etiology
  • Acquired Immunodeficiency Syndrome / immunology
  • Amino Acid Sequence
  • CD4-Positive T-Lymphocytes / microbiology
  • Cross-Linking Reagents
  • Cytopathogenic Effect, Viral
  • HIV Envelope Protein gp41 / metabolism*
  • HIV-1 / immunology*
  • Humans
  • Lymphocyte Activation
  • Molecular Sequence Data
  • Receptors, Virus / analysis*
  • Recombinant Proteins / immunology
  • Sensitivity and Specificity
  • Tumor Cells, Cultured

Substances

  • Cross-Linking Reagents
  • HIV Envelope Protein gp41
  • Receptors, Virus
  • Recombinant Proteins