Analysis of the interaction of antibodies with a conserved enzymatically deglycosylated core of the HIV type 1 envelope glycoprotein 120. Academic Article uri icon

Overview

abstract

  • The binding of a panel of monoclonal antibodies to V1, V2, and V3 loop-deleted HIV-1 gp120 was studied by competition analysis. Most of the previously defined relationships between gp120 epitopes were preserved on the variable loop-deleted protein, although interactions between some epitopes were dependent on the presence of the V1, V2, and V3 loops. Enzymatic deglycosylation of the variable loop-deleted protein only minimally altered the binding of most antibodies examined. Thus, a carbohydrate-deficient, conserved HIV-1 gp120 core can be produced that has a structure closely approximating that of the full-length, correctly folded gp120 monomer.

publication date

  • February 10, 1998

Research

keywords

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

Identity

Scopus Document Identifier

  • 0032501955

Digital Object Identifier (DOI)

  • 10.1089/aid.1998.14.191

PubMed ID

  • 9491908

Additional Document Info

volume

  • 14

issue

  • 3