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Functional complementation of a model target to study Vpu sensitivity.

Sanath Kumar Janaka1, Jared Faurot, Marc C Johnson

  • 1Department of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri, United States of America.

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Summary
This summary is machine-generated.

The HIV-1 accessory protein Vpu prevents Gibbon ape Leukemia Virus (GaLV) Env incorporation into viral particles. A single GaLV cytoplasmic tail domain (CTD) in an Env trimer is sufficient for Vpu sensitivity, provided it

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Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Human Immunodeficiency Virus type 1 (HIV-1) Env normally incorporates into infectious virions.
  • HIV-1 Env is incompatible with Gibbon ape Leukemia Virus (GaLV) Env, hindering particle formation.
  • The HIV-1 accessory protein Vpu is identified as the cause of this incompatibility, blocking GaLV Env incorporation.

Purpose of the Study:

  • To investigate the structural requirements of the GaLV Env cytoplasmic tail domain (CTD) for Vpu-mediated incorporation into HIV-1 particles.
  • To determine if all three helical regions within the Env trimer's CTD must possess the Vpu sensitivity motif for Vpu to modulate incorporation.

Main Methods:

  • Utilized functional complementation assays with Murine Leukemia Virus (MLV) and chimeric MLV/GaLV Env mutants.
  • Created and analyzed mixed trimers containing both MLV and GaLV CTDs, as well as trimers with only one GaLV CTD.
  • Assessed viral particle infectivity and Env incorporation sensitivity to Vpu.

Main Results:

  • Mixed trimers with both MLV and GaLV CTDs were functional and sensitive to Vpu.
  • Trimers with one GaLV CTD and one lacking a CTD remained functional but were resistant to Vpu.
  • These findings indicate a specific requirement for the trimeric CTD complex for Vpu sensitivity.

Conclusions:

  • The presence of at least one GaLV CTD in an Env trimer is sufficient to confer Vpu sensitivity.
  • Vpu sensitivity requires the GaLV CTD to be part of a complete trimeric CTD complex.
  • This study elucidates the structural basis for Vpu-mediated regulation of Env incorporation in retroviral particles.