Neutralization of the human immunodeficiency virus type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex. Academic Article uri icon

Overview

abstract

  • To test whether antibodies that are neutralizing or nonneutralizing for human immunodeficiency virus type 1 (HIV-1) primary isolates can be distinguished by their affinities for the oligomeric envelope glycoproteins, we selected HIV-1(JR-FL) as a model primary virus and a panel of 13 human monoclonal antibodies (MAbs) and evaluated three parameters: (i) half-maximal binding to recombinant monomeric envelope, gp120(JR-FL); (ii) half-maximal binding to oligomeric envelope of HIV-1(JR-FL) expressed on the surface of transfected 293 cells; and (iii) neutralization of HIV-1(JR-FL) in a peripheral blood mononuclear cell-based neutralization assay. Two conclusions can be drawn from these experiments. First, we confirm that antibody interactions with monomeric gp120 do not predict primary virus neutralization. Second, we show that neutralization correlates qualitatively with the relative affinity of an antibody for the oligomeric envelope glycoproteins, at least for HIV-1(JR-FL).

publication date

  • April 1, 1997

Research

keywords

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

Identity

PubMed Central ID

  • PMC191401

Scopus Document Identifier

  • 0030897825

Digital Object Identifier (DOI)

  • 10.1128/JVI.71.4.2779-2785.1997

PubMed ID

  • 9060632

Additional Document Info

volume

  • 71

issue

  • 4