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Related Experiment Videos

Structural principles controlling HIV envelope glycosylation.

Anna-Janina Behrens1, Max Crispin2

  • 1Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.

Current Opinion in Structural Biology
|April 1, 2017
PubMed
Summary
This summary is machine-generated.

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The HIV-1 envelope protein

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • The human immunodeficiency virus type 1 (HIV-1) envelope (Env) protein is the primary target for antibody-mediated vaccine development due to its surface exposure on virions.
  • Env's dense glycosylation and trimeric structure create steric constraints, leading to immature glycan structures and a conserved 'trimer-induced mannose patch'.

Purpose of the Study:

  • To define the steric principles governing glycan processing on the HIV-1 Env protein.
  • To map the glycan shield of the trimeric HIV-1 Env spike.

Main Methods:

  • Quantitative mass spectrometry of glycopeptides.
  • Structural analysis of the trimeric viral spike.

Main Results:

Related Experiment Videos

  • Dense glycosylation and trimerization sterically hinder enzymatic processing of Env glycans, resulting in immature oligomannose structures.
  • A significant 'trimer-induced mannose patch' is formed by these sterically constrained glycans.
  • These immature glycans represent a conserved viral feature targeted by broadly neutralizing antibodies.

    • Conclusions:

    • The study elucidates how Env structure dictates glycan processing and creates a conserved target for antibody recognition.
    • Understanding the glycan shield is crucial for designing effective HIV-1 vaccines.