Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. Academic Article uri icon

Overview

abstract

  • We have isolated and characterized human monoclonal antibody 2G12 to the gp120 surface glycoprotein of human immunodeficiency virus type 1 (HIV-1). This antibody potently and broadly neutralizes primary and T-cell line-adapted clade B strains of HIV-1 in a peripheral blood mononuclear cell-based assay and inhibits syncytium formation in the AA-2 cell line. Furthermore, 2G12 possesses neutralizing activity against strains from clade A but not from clade E. Complement- and antibody-dependent cellular cytotoxicity-activating functions of 2G12 were also defined. The gp120 epitope recognized by 2G12 was found to be distinctive; binding of 2G12 to LAI recombinant gp120 was abolished by amino acid substitutions removing N-linked carbohydrates in the C2, C3, V4, and C4 regions of gp120. This gp120 mutant recognition pattern has not previously been observed, indicating that the 2G12 epitope is unusual. consistent with this, antibodies able to block 2G12 binding to recombinant gp120 were not detected in significant quantities in 16 HIV-positive human serum samples.

publication date

  • February 1, 1996

Research

keywords

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

Identity

PubMed Central ID

  • PMC189917

Scopus Document Identifier

  • 9044241681

Digital Object Identifier (DOI)

  • 10.1128/JVI.70.2.1100-1108.1996

PubMed ID

  • 8551569

Additional Document Info

volume

  • 70

issue

  • 2