Crystal structure of a soluble cleaved HIV-1 envelope trimer Academic Article uri icon

Overview

MeSH Major

  • env Gene Products, Human Immunodeficiency Virus

abstract

  • HIV-1 entry into CD4(+) target cells is mediated by cleaved envelope glycoprotein (Env) trimers that have been challenging to characterize structurally. Here, we describe the crystal structure at 4.7 angstroms of a soluble, cleaved Env trimer that is stabilized and antigenically near-native (termed the BG505 SOSIP.664 gp140 trimer) in complex with a potent broadly neutralizing antibody, PGT122. The structure shows a prefusion state of gp41, the interaction between the component gp120 and gp41 subunits, and how a close association between the gp120 V1/V2/V3 loops stabilizes the trimer apex around the threefold axis. The complete epitope of PGT122 on the trimer involves gp120 V1, V3, and several surrounding glycans. This trimer structure advances our understanding of how Env functions and is presented to the immune system, and provides a blueprint for structure-based vaccine design.

publication date

  • January 2013

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC3886632

Digital Object Identifier (DOI)

  • 10.1126/science.1245625

PubMed ID

  • 24179159

Additional Document Info

start page

  • 1477

end page

  • 83

volume

  • 342

number

  • 6165