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Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers

Academic Article
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Overview

related to degree

  • Lee, Jeong Hyun, Ph.D. in Chemical Biology, Scripps Research 2011 - 2016

authors

  • Khayat, R.
  • Lee, Jeong Hyun
  • Julien, J. P.
  • Cupo, A.
  • Klasse, P. J.
  • Sanders, R. W.
  • Moore, J. P.
  • Wilson, Ian
  • Ward, Andrew

publication date

  • September 2013

journal

  • Journal of Virology  Journal

abstract

  • Human immunodeficiency virus type 1 (HIV-1) infection is a significant global public health problem for which development of an effective prophylactic vaccine remains a high scientific priority. Many concepts for a vaccine are focused on induction of appropriate titers of broadly neutralizing antibodies (bNAbs) against the viral envelope (Env) glycoproteins gp120 and gp41, but no immunogen has yet accomplished this goal in animals or humans. One approach to induction of bNAbs is to design soluble, trimeric mimics of the native viral Env trimer. Here, we describe structural studies by negative-stain electron microscopy of several variants of soluble Env trimers based on the KNH1144 subtype A sequence. These Env trimers are fully cleaved between the gp120 and gp41 components and stabilized by specific amino acid substitutions. We also illustrate the structural consequences of deletion of the V1/V2 and V3 variable loops from gp120 and the membrane-proximal external region (MPER) from gp41. All of these variants adopt a trimeric configuration that appropriately mimics native Env spikes, including the CD4 receptor-binding site and the epitope for the VRC PG04 bNAb. These cleaved, soluble trimer designs can be adapted for use with multiple different env genes for both vaccine and structural studies.

subject areas

  • AIDS Vaccines
  • Amino Acid Substitution
  • Antibodies, Neutralizing
  • Antigens, CD4
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp41
  • HIV-1
  • Humans
  • Imaging, Three-Dimensional
  • Models, Molecular
  • Molecular Mimicry
  • Protein Structure, Quaternary
  • Solubility
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Identity

PubMed Central ID

  • PMC3754114

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.01222-13

PubMed ID

  • 23824817
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Additional Document Info

start page

  • 9865

end page

  • 9872

volume

  • 87

issue

  • 17

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