Rat monoclonal antibodies to nonoverlapping epitopes of human immunodeficiency virus type 1 gp120 block CD4 binding in Vitro Academic Article Article uri icon


MeSH Major

  • Esophageal Achalasia
  • Esophagoscopy
  • Natural Orifice Endoscopic Surgery
  • Tomography, Optical Coherence


  • Monoclonal antibodies (MAbs) to a recombinant form of the envelope glycoprotein gp120 of human immunodeficiency virus type 1 (HIV-1 IIIB) were raised in rats and screened for their ability to block recombinant gp120 binding to recombinant, soluble CD4 (sCD4) in vitro. Four such MAbs were identified and characterised. Each MAb bound strongly to gp120 from eight widely divergent HIV-1 strains from the United States and Africa. Two MAbs were mapped to the fourth conserved (C4) region of gp120, whereas the other two recognised an as yet undefined, conformationally sensitive epitope. MAbs to the latter epitope were the more potent in blocking the gp120-sCD4 interaction. None of the MAbs, however, had potent neutralising activity.

publication date

  • January 1991



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1016/0042-6822(91)90755-Z

PubMed ID

  • 1718090

Additional Document Info

start page

  • 72

end page

  • 9


  • 185


  • 1