Molecular Architecture of the cleavage- dependent mannose patch on a soluble HIV-1 envelope glycoprotein trimer Academic Article uri icon

Overview

MeSH Major

  • HIV-1
  • Mannose
  • Models, Molecular
  • Protein Conformation
  • Protein Multimerization
  • env Gene Products, Human Immunodeficiency Virus

abstract

  • The envelope spike of human immunodeficiency virus type 1 (HIV-1) is a target for antibody-based neutralization. For some patients infected with HIV-1, highly potent antibodies have been isolated that can neutralize a wide range of circulating viruses. It is a goal of HIV-1 vaccine research to elicit these antibodies by immunization with recombinant mimics of the viral spike. These antibodies have evolved to recognize the dense array of glycans that coat the surface of the viral molecule. We show how the structure of these glycans is shaped by steric constraints imposed upon them by the native folding of the viral spike. This information is important in guiding the development of vaccine candidates.

publication date

  • January 2017

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC5215339

Digital Object Identifier (DOI)

  • 10.1128/JVI.01894-16

PubMed ID

  • 27807235

Additional Document Info

volume

  • 91

number

  • 2