Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy Academic Article uri icon

Overview

MeSH Major

  • HIV Antibodies
  • Immunoglobulin Fab Fragments
  • Macromolecular Substances
  • env Gene Products, Human Immunodeficiency Virus

abstract

  • HIV-1 is a human virus that results in the deaths of millions of people around the world each year. While there are several effective therapeutics available to prolong life, a vaccine is the best long-term solution for curbing this global epidemic. Here, we present structural data that reveal the viral binding site of one of the first HIV-1-neutralizing antibodies isolated, 2G12, and provide a rationale for its effectiveness. These structures provide a basis for higher-resolution studies to determine the molecular nature of the 2G12 epitope, which will aid in vaccine design and antibody-based therapies.

publication date

  • September 2014

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC4136306

Digital Object Identifier (DOI)

  • 10.1128/JVI.01229-14

PubMed ID

  • 24965454

Additional Document Info

start page

  • 10177

end page

  • 88

volume

  • 88

number

  • 17