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Hiv-1 neutralization: Mechanisms and relevance to vaccine design

Academic Article
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Overview

authors

  • Zwick, Michael
  • Burton, Dennis

publication date

  • November 2007

journal

  • Current HIV Research  Journal

abstract

  • Antibody (Ab) mediated neutralization is a crucial means of host resistance to many pathogens and will most likely be required in the development of a vaccine to protect against HIV-1. Here we examine mechanistic aspects of HIV-1 neutralization with attention to recent studies on the stoichiometric, kinetic and thermodynamic parameters involved. Neutralization of HIV-1, as with any microbe, minimally requires an initial molecular encounter with Ab. Ab occupancy of functional heterotrimers of the envelope glycoproteins, gp120 and gp41 (Env), indeed appears to be the dominant mechanism of neutralization for HIV-1. However, the Ab-binding site, the parameters mentioned above, as well as the stages and duration of vulnerability to Ab recognition, prior to and leading up to viral entry, each have a distinct impact on the mechanism of neutralization for any given Ab specificity. With HIV-1, the problems of mutational variation and neutralization resistance, coupled with the lability and conformational heterogeneity in Env, have stimulated the search for rational approaches to Env immunogen design that are unprecedented in vaccinology.

subject areas

  • AIDS Vaccines
  • Antibody Specificity
  • Antigen-Antibody Reactions
  • Antigens, CD4
  • Drug Design
  • Epitopes
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp41
  • HIV Infections
  • HIV-1
  • Host-Pathogen Interactions
  • Humans
  • Vaccines, Synthetic
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Research

keywords

  • antibodies
  • neutralization mechanism
  • vaccine development
  • virus fusion
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Identity

International Standard Serial Number (ISSN)

  • 1570-162X

Digital Object Identifier (DOI)

  • 10.2174/157016207782418443

PubMed ID

  • 18045117
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Additional Document Info

start page

  • 608

end page

  • 624

volume

  • 5

issue

  • 6

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