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Determination of Molecular Structures of HIV Envelope Glycoproteins using Cryo-Electron Tomography and Automated Sub-tomogram Averaging
Published on: December 1, 2011
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Computational characterization of HIV envelope interactions with cellular GRP78 as a potential entry mechanism
Wael M Elshemey1, Hamdy I A Mostafa2, Abdo A Elfiky2
1Department of Physics, Faculty of Sciences, Islamic University in Madinah, Madinah 42351, Saudia Arabia.
Cell Stress & Chaperones
|November 5, 2025
Summary
Human Immunodeficiency Virus (HIV) uses its envelope protein to bind to glucose-regulated protein 78 (GRP78) on host cells. The R4 region of the HIV envelope protein is identified as a key binding site for GRP78.
Area of Science:
- Virology
- Structural Biology
- Computational Biology
Background:
- Human Immunodeficiency Virus (HIV) infection remains a global health concern.
- HIV utilizes its envelope protein to interact with host cells.
- Glucose-regulated protein 78 (GRP78) is overexpressed in stressed cells and serves as a potential binding target for HIV.
Purpose of the Study:
- To investigate the binding interaction between the HIV envelope protein and GRP78.
- To identify specific binding sites on the HIV envelope protein for GRP78.
Main Methods:
- Utilized a comprehensive in silico approach.
- Performed protein-protein docking simulations.
- Conducted molecular dynamics simulations (MDS).
Main Results:
- Identified the R4 region (C388-C418) of the HIV envelope protein as the potential binding site for GRP78.
- Calculated an average binding energy of -12.20 ± 2.0 kcal/mol for the R4 region interaction.
- Confirmed GRP78 as a cell surface binding target for the HIV envelope protein.
Conclusions:
- The R4 region is a critical binding site for HIV envelope protein interaction with GRP78.
- These findings provide a basis for developing novel inhibitors targeting viral entry.
- Further research may lead to strategies to combat HIV infection by blocking host cell recognition.
