Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. Academic Article uri icon

Overview

abstract

  • Forty-six monoclonal antibodies (MAbs) able to bind to the native, monomeric gp120 glycoprotein of the human immunodeficiency virus type 1 (HIV-1) LAI (HXBc2) strain were used to generate a competition matrix. The data suggest the existence of two faces of the gp120 glycoprotein. The binding sites for the viral receptor, CD4, and neutralizing MAbs appear to cluster on one face, which is presumably exposed on the assembled, oligomeric envelope glycoprotein complex. A second gp120 face, which is presumably inaccessible on the envelope glycoprotein complex, contains a number of epitopes for nonneutralizing antibodies. This analysis should be useful for understanding both the interaction of antibodies with the HIV-1 gp120 glycoprotein and neutralization of HIV-1.

publication date

  • March 1, 1996

Research

keywords

  • Antibodies, Monoclonal
  • Antibodies, Viral
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • HIV-1

Identity

PubMed Central ID

  • PMC190014

Scopus Document Identifier

  • 0030043169

Digital Object Identifier (DOI)

  • 10.1128/JVI.70.3.1863-1872.1996

PubMed ID

  • 8627711

Additional Document Info

volume

  • 70

issue

  • 3