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Conserved changes in envelope function during human immunodeficiency virus type 1 coreceptor switching.

Cristina Pastore1, Rebecca Nedellec, Alejandra Ramos

  • 1Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Journal of Virology
|May 18, 2007
PubMed
Summary
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Understanding human immunodeficiency virus type 1 (HIV-1) coreceptor switching reveals key envelope changes. HIV-1 envelope mutations during CCR5 to CXCR4 switching show decreased CCR5 and increased CD4 binding, impacting inhibitor sensitivity.

Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • Human immunodeficiency virus type 1 (HIV-1) entry into host cells relies on the envelope (Env) glycoprotein binding to CD4 and a coreceptor, either CCR5 or CXCR4.
  • Coreceptor tropism switching, from CCR5 (R5) to CXCR4 (X4), is a critical step in HIV-1 pathogenesis and influences viral tropism and therapeutic responses.

Purpose of the Study:

  • To investigate the functional and binding alterations of the HIV-1 envelope during the transition from CCR5 to CXCR4 coreceptor utilization.
  • To characterize intermediate envelope mutants for their sensitivity to entry inhibitors and neutralizing antibodies.

Main Methods:

  • Site-directed mutagenesis was employed to generate four distinct series of HIV-1 envelope mutants mimicking coreceptor switch intermediates.
  • Mutant envelopes were assessed for their utilization of CCR5 and CXCR4, sensitivity to CCR5/CXCR4 inhibitors (e.g., AMD3100), soluble CD4, and neutralizing antibodies (b12-IgG, 4E10).

Related Experiment Videos

  • Binding assays (CD4, CCR5) and fusion assays were performed on a subset of mutants.

    • Main Results:

    • Coreceptor switch intermediates exhibited increased sensitivity to CCR5 inhibitors, correlating with reduced CCR5 binding.
    • As CXCR4 utilization increased, mutants showed enhanced resistance to soluble CD4 inhibition and increased CD4 binding.
    • Mutants displayed increasing resistance to the CXCR4 inhibitor AMD3100, with variable sensitivity to neutralizing antibodies.
    • Functional changes were consistent across all mutant series, irrespective of the final coreceptor preference.

    Conclusions:

    • Decreased CCR5 binding and increased CD4 binding are common characteristics of HIV-1 envelope intermediates during coreceptor switching.
    • These envelope modifications during the CCR5-to-CXCR4 switch influence viral sensitivity to entry inhibitors and neutralizing antibodies.
    • Understanding these evolutionary changes provides insights into HIV-1 tropism and potential therapeutic strategies.