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CCR5 structural plasticity shapes HIV-1 phenotypic properties.

Philippe Colin1,2,3, Zhicheng Zhou1,2, Isabelle Staropoli1,2

  • 1Viral Pathogenesis Unit, Department of Virology, Institut Pasteur, Paris, France.

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HIV-1 envelope proteins bind diverse CCR5 forms, influencing viral entry and tropism. CCR5 structural variations impact HIV-1 infection, suggesting new drug targets for CCR5-based therapies.

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Area of Science:

  • Immunology
  • Virology
  • Structural Biology

Background:

  • CCR5 is a key coreceptor for R5 HIV-1 strains, mediating viral entry into host cells.
  • CCR5 exhibits significant structural diversity, existing in various conformations and oligomerization states.
  • The functional implications of CCR5's structural heterogeneity in HIV-1 infection remain incompletely understood.

Purpose of the Study:

  • To investigate the role of CCR5 structural diversity in HIV-1 infection.
  • To determine how different HIV-1 envelope glycoproteins (gp120s) interact with distinct CCR5 populations.
  • To elucidate the impact of CCR5 conformation and oligomerization on viral entry and tropism.

Main Methods:

  • Analysis of gp120 binding to CCR5 on various cell types.
  • Characterization of CCR5 conformations and oligomerization states.
  • Functional assays assessing viral entry and inhibition by CCR5 ligands.
  • Mutagenesis of the CCR5 dimerization interface.

Main Results:

  • HIV-1 gp120s exhibit differential binding to distinct CCR5 populations, which vary in expression and conformation.
  • CCR5 oligomerization status modulates gp120 binding and viral entry, with a preference for monomers.
  • Differences in CCR5 populations between T-cells and macrophages correlate with differential gp120 binding and viral tropism.
  • CCR5 structural plasticity is crucial for the entry of certain R5 HIV-1 isolates, particularly in macrophages.

Conclusions:

  • CCR5 heterogeneity diversifies HIV-1 phenotypic properties, influencing viral tropism and drug sensitivity.
  • Specific CCR5 conformations are utilized by different HIV-1 strains for entry.
  • Understanding CCR5 structural dynamics offers new avenues for developing targeted HIV-1 therapies.