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Related Experiment Videos

Antigenically distinct conformations of CXCR4.

F Baribaud1, T G Edwards, M Sharron

  • 1Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.

Journal of Virology
|September 5, 2001
PubMed
Summary

Human immunodeficiency virus type 1 (HIV-1) entry is influenced by coreceptor CXCR4 conformation. CXCR4 exists in multiple forms, affecting HIV-1 infection and drug development.

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[Fusion and hemifusion induced by wild type (WT) and mutant (W596M) envelope glycoproteins of HIV].

Virologie (Montrouge, France)·2021

Area of Science:

  • Immunology
  • Virology
  • Cell Biology

Background:

  • Human immunodeficiency virus type 1 (HIV-1) entry into host cells relies on CD4 and coreceptors like CCR5 and CXCR4.
  • Viral tropism is largely determined by coreceptor expression and usage, but other factors like receptor conformation may play a role.
  • Seven-transmembrane domain receptors, including CXCR4, can exhibit conformational heterogeneity, the impact of which on HIV-1 infection is unclear.

Purpose of the Study:

  • To investigate the conformational heterogeneity of the HIV-1 coreceptor CXCR4 on different cell types.
  • To determine if CXCR4 conformational heterogeneity influences its interaction with antibodies and its role in HIV-1 infection.
  • To identify factors that may regulate CXCR4 conformation.

Main Methods:

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  • Utilized a panel of monoclonal antibodies (MAbs) targeting CXCR4.
  • Analyzed CXCR4 conformation on primary T cells, transformed T cells, and primary B cells.
  • Assessed the impact of conformational heterogeneity on antibody binding, chemotaxis inhibition, and HIV-1 infection inhibition.

    • Main Results:

    • CXCR4 displayed significant conformational heterogeneity across various primary and transformed T and B cells.
    • The commonly used MAb 12G5 recognizes only a subset of CXCR4 molecules, leading to underestimation of CXCR4 expression levels.
    • CXCR4 conformational heterogeneity explains cell-type-specific variations in antibody-mediated inhibition of chemotaxis and HIV-1 infection.
    • Alterations in CXCR4 conformation are not linked to glycosylation, N-terminal sulfation, or G-protein coupling.

    Conclusions:

    • CXCR4 exists in multiple conformations, impacting its function as an HIV-1 coreceptor.
    • The conformational state of CXCR4 influences its interaction with blocking antibodies and viral entry.
    • Understanding CXCR4 conformational dynamics is crucial for developing effective HIV-1 entry inhibitors and receptor antagonists.