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Related Experiment Videos

A conformational switch controlling HIV-1 morphogenesis.

I Gross1, H Hohenberg, T Wilk

  • 1Heinrich-Pette-Institut für experimentelle Virologie und Immunologie an der Universität Hamburg, Martinistrasse 52, D-20251 Hamburg, Germany.

The EMBO Journal
|January 5, 2000
PubMed
Summary
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Human immunodeficiency virus type 1 (HIV-1) assembly involves Gag protein forming spherical immature capsids. Spacer peptide SP1 acts as a switch, enabling spherical assembly and its cleavage leading to mature conical capsids.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Human immunodeficiency virus type 1 (HIV-1) assembly is a complex process crucial for viral infectivity.
  • Immature HIV-1 virions possess a spherical capsid composed of uncleaved Gag polyproteins.
  • Proteolytic processing and rearrangement of the capsid lead to the mature, infectious conical core.

Purpose of the Study:

  • To investigate the role of HIV-1 Gag protein in capsid assembly.
  • To determine the influence of specific protein domains on capsid morphology.
  • To elucidate the mechanism by which Gag assembly transitions from immature to mature forms.

Main Methods:

  • Utilized an in vitro assembly system with HIV-1 Gag-derived proteins.
  • Analyzed particle morphology (spherical, tubular, conical) using techniques like electron microscopy (implied).

Related Experiment Videos

  • Assessed protein conformation through differential binding to capsid protein (CA) specific monoclonal antibodies.

    • Main Results:

    • Demonstrated that a single HIV-1 Gag-derived protein can form spherical, tubular, or conical particles in vitro.
    • Correlated assembly phenotypes with distinct conformations of the CA domain, indicated by antibody binding.
    • Showed that the absence of spacer peptide SP1 resulted exclusively in tubular and conical particle formation.

    Conclusions:

    • HIV-1 Gag protein can adopt different conformations influencing capsid assembly.
    • Spacer peptide SP1 acts as a critical molecular switch regulating capsid morphology.
    • SP1's presence promotes spherical immature capsid formation, while its cleavage facilitates maturation into conical capsids.