Related Experiment Video
Updated: Jun 28, 2026
07:10
Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Published on: September 14, 2014
Conformational variability of HIV-1 Env trimer and viral vulnerability
1Department of Biological Sciences, Lehigh University, Bethlehem, United States.
Elife
|June 26, 2026
Summary
The Human Immunodeficiency Virus type 1 (HIV-1) envelope glycoprotein (Env) ectodomain is stable, while its membrane-proximal external region (MPER) allows flexibility for receptor engagement. This study models the full Env trimer to understand HIV entry mechanisms.
Area of Science:
- Structural biology
- Virology
- Computational biophysics
Background:
- The Human Immunodeficiency Virus type 1 (HIV-1) envelope glycoprotein (Env) is crucial for viral entry and a key target for vaccines and antivirals.
- Previous studies often analyzed Env's ectodomain and transmembrane domain (TMD) separately, with limited structural data on the cytoplasmic tail (CT).
Purpose of the Study:
- To investigate the full-length, glycosylated HIV-1 gp120-gp41 trimer as a complete entity using molecular dynamics simulations.
- To understand the structural flexibility and dynamics of the HIV-1 Env trimer within a lipid bilayer.
Main Methods:
- Construction of a fully glycosylated, full-length gp120-gp41 trimer model embedded in a lipid bilayer.
- All-atom molecular dynamics simulations to analyze structural stability, flexibility, and interactions.
Main Results:
- The Env ectodomain exhibits a stable prefusion structure, while the MPER's flexibility allows varied orientations for receptor binding.
- The TMD's R696 residue interacts with lipids, ions, and the CT, causing conformational changes and membrane perturbations that may aid fusion.
- Simulation trajectories provide insights into antibody epitope accessibility across the Env trimer.
Conclusions:
- The study provides a comprehensive structural and dynamic view of the complete HIV-1 Env trimer.
- The findings highlight the roles of MPER flexibility and TMD-CT interactions in HIV fusion and offer a framework for epitope accessibility analysis.
Keywords:
HIV envelopeantibodyglycangp120–gp41molecular biophysicsmolecular dynamics simulationstructural biologyvirusesMore Related Videos
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