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  3. Controlling Spatial Organization Of Hiv Coreceptor Ccr5.
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  3. Controlling Spatial Organization Of Hiv Coreceptor Ccr5.

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Controlling Spatial Organization of HIV Coreceptor CCR5.

Shivam Gupta1, Taraknath Mandal1

  • 1Department of Physics, Indian Institute of Technology Kanpur, Kanpur-208016, India.

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|March 9, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

CC chemokine receptor type 5 (CCR5) is crucial for HIV entry. Molecular dynamics simulations show lysophosphatidylcholine (lysoPC) disrupts CCR5 organization at membrane boundaries, potentially blocking HIV fusion.

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Area of Science:

  • Biophysics
  • Cellular Biology
  • Virology

Background:

  • CC chemokine receptor type 5 (CCR5) is a primary coreceptor for HIV entry into host cells.
  • CCR5 localization at lipid domain boundaries enhances HIV fusion efficiency by facilitating gp41 interaction with membrane interfaces.
  • Understanding CCR5's spatial organization is key to developing strategies against HIV entry.

Purpose of the Study:

  • To investigate the spatial organization of CCR5 in domain-forming model membranes using molecular dynamics simulations.
  • To elucidate the molecular mechanism of CCR5 localization at membrane domain boundaries.
  • To explore the effect of lysophosphatidylcholine (lysoPC) lipids on CCR5 organization and membrane properties.

Main Methods:

  • Coarse-grained molecular dynamics simulations were employed to model CCR5 within heterogeneous lipid membranes.
  • Analysis focused on the preferential localization and stabilization of CCR5 at lipid domain interfaces.
  • The impact of lysoPC, acting as a linactant, on membrane domain organization and CCR5 distribution was simulated.

    • Main Results:

    • Simulations revealed that CCR5 preferentially migrates to and stabilizes at the boundaries of lipid domains.
    • Lysophosphatidylcholine (lysoPC) lipids were observed to accumulate at domain interfaces, reducing line tension.
    • This accumulation of lysoPC disrupted membrane domain organization, leading to CCR5 delocalization.

    Conclusions:

    • CCR5's preferential localization at membrane domain boundaries is a key factor in facilitating HIV fusion.
    • Linactants like lysoPC can disrupt membrane organization and delocalize CCR5, potentially hindering HIV entry.
    • Targeting CCR5 organization via linactants presents a potential therapeutic strategy to inhibit HIV fusion and entry.