Interactions of polyclonal and monoclonal anti-glycoprotein 120 antibodies with oligomeric glycoprotein 120-glycoprotein 41 complexes of a primary HIV type 1 isolate: relationship to neutralization. Academic Article uri icon

Overview

abstract

  • We have studied antibody reactivity with monomeric and oligomeric forms of the gp120 envelope glycoprotein from the macrophage-tropic primary virus, HIV-1 JR-FL. We find that the correlation between oligomer reactivity and virus neutralization is not absolute for MAbs to epitopes overlapping the CD4-binding site on gp120. An MAb (205-46-9) with very limited neutralizing ability for JR-FL binds about as avidly to oligomeric JR-FL envelope glycoproteins as the strongly neutralizing IgG1b12 MAb does. In addition, neutralizing and nonneutralizing sera from HIV-1-infected people are similar in their reactivities to oligomeric JR-FL envelope glycoproteins; the correlation between oligomer reactivity and virus neutralization is weak. Although oligomer reactivity of an anti-gp120 antibody is necessary for virus neutralization, it is not always sufficient to cause it.

publication date

  • May 1, 1998

Research

keywords

  • HIV Antibodies
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp41
  • HIV-1
  • Oligopeptides

Identity

Scopus Document Identifier

  • 0032080445

Digital Object Identifier (DOI)

  • 10.1089/aid.1998.14.591

PubMed ID

  • 9591713

Additional Document Info

volume

  • 14

issue

  • 7