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Updated: Apr 18, 2026

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

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

Published on: September 14, 2014

A new ensemble coevolution system for detecting HIV-1 protein coevolution.

Guangdi Li¹, Kristof Theys², Jens Verheyen³

¹KU Leuven - University of Leuven, Department of Microbiology and Immunology, Rega Institute for Medical Research, Clinical and Epidemiological Virology, Leuven, Belgium. liguangdi.research@gmail.com.

|January 8, 2015

Summary

An ensemble system combining 27 methods improves detection of coevolving amino acids in HIV-1 proteins. This approach identified key coevolving residues within structural proteins and between Gag and protease, aiding understanding of HIV-1 evolution.

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Last Updated: Apr 18, 2026

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Published on: September 14, 2014

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Prediction of HIV-1 Coreceptor Usage Tropism by Sequence Analysis using a Genotypic Approach

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Published on: December 1, 2011

Area of Science:

Molecular Biology
Bioinformatics
Virology

Background:

Identifying coevolving amino acids in HIV-1 proteins is crucial for understanding molecular evolution.
Existing sequence-based methods for detecting coevolution have limitations.
An integrated system for HIV-1 protein coevolution detection has been lacking.

Purpose of the Study:

To develop and evaluate an ensemble coevolution system for detecting position-specific coevolution in HIV-1 proteins.
To improve the accuracy of HIV-1 intra- and inter-protein coevolution predictions.
To identify key coevolving residues within HIV-1 structural proteins and between Gag and protease.

Main Methods:

Integrated 27 sequence-based prediction methods into an ensemble coevolution system.
Evaluated individual and combined methods using HIV-1 protein structures and experimental data.
Analyzed HIV-1 intra- and inter-protein coevolution, focusing on Gag and protease.

Main Results:

The ensemble system allowed combinations of different sequence-based methods for coevolution predictions.
A combination of four methods outperformed individual methods in predicting HIV-1 coevolution.
Coevolving positions were found in functional domains and physically contacted in tertiary structures.
Protease drug resistance positions coevolved with Gag cleavage and C-terminal positions under selective pressure.

Conclusions:

Developed a novel ensemble coevolution system using 27 sequence-based methods.
Highlighted key coevolving residues within HIV-1 structural proteins.
Provided insights into HIV-1 intra- and inter-protein coevolution, particularly between Gag and protease.