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Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

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Cholesterol Mediates Gp41 Linear Aggregation and Enhanced Membrane Curvature during HIV-1 Infection.

Junyi Zhao¹, Yang Jiang¹, Li Zhao²

¹State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun 130012, China.

The Journal of Physical Chemistry. B

|February 17, 2026

Summary

Cholesterol alters HIV-1 gp41 structure, promoting linear aggregation and membrane curvature. This lipid-driven mechanism enhances viral entry and suggests new fusion inhibition strategies.

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Published on: March 8, 2012

Area of Science:

Biophysics
Virology
Membrane Biology

Background:

HIV-1 entry relies on envelope glycoprotein gp41 and membrane fusion.
Cholesterol is crucial for HIV-1 infectivity, but its role in gp41 function is unclear.

Purpose of the Study:

To investigate how cholesterol concentration affects gp41 dynamics and membrane remodeling.
To elucidate the molecular mechanisms of cholesterol-mediated gp41 clustering and viral entry facilitation.

Main Methods:

Molecular dynamics simulations were used to model gp41 behavior in lipid bilayers.
Simulations varied cholesterol concentrations to observe effects on protein structure and membrane curvature.

Main Results:

Cholesterol induces an umbrella-like conformation in gp41, favoring linear aggregation over compact clusters.
Cholesterol amplifies local membrane curvature around gp41 clusters.
High cholesterol (≥30%) drives formation of highly curved membrane structures, increasing gp41 density and cluster stability.

Conclusions:

Cholesterol modulates gp41 interactions and membrane thickness, leading to increased curvature and protein clustering.
Findings provide a molecular framework for cholesterol's role in HIV-1 entry.
This research suggests novel strategies for inhibiting viral fusion by targeting cholesterol-gp41 interactions.