Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 env trimers Academic Article uri icon

Overview

MeSH Major

  • Antibodies, Monoclonal
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp41

abstract

  • All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we define and structurally characterize a unique epitope on Env that is recognized by a recently discovered family of human monoclonal antibodies (PGT151-PGT158). The PGT151 epitope is comprised of residues and glycans at the interface of gp41 and gp120 within a single protomer and glycans from both subunits of a second protomer and represents a neutralizing epitope that is dependent on both gp120 and gp41. Because PGT151 binds only to properly formed, cleaved trimers, this distinctive property, and its ability to stabilize Env trimers, has enabled the successful purification of mature, cleaved Env trimers from the cell surface as a complex with PGT151. Here we compare the structural and functional properties of membrane-extracted Env trimers from several clades with those of the soluble, cleaved SOSIP gp140 trimer.

publication date

  • May 15, 2014

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC4057017

Digital Object Identifier (DOI)

  • 10.1016/j.immuni.2014.04.008

PubMed ID

  • 24768348

Additional Document Info

start page

  • 669

end page

  • 80

volume

  • 40

number

  • 5