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Updated: May 5, 2026
Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Published on: September 14, 2014
Modeling virus- and antibody-specific factors to predict human immunodeficiency virus neutralization efficiency
Hillel Haim1, Ignacio Salas, Kathleen McGee
1Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02215, USA; Department of Microbiology, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.
Understanding human immunodeficiency virus type 1 (HIV-1) neutralization requires analyzing viral and antibody factors. A new model explains how antibody binding and viral envelope glycoprotein (Env) variations affect HIV-1 neutralization efficacy.
Area of Science:
- Immunology
- Virology
- Computational Biology
Background:
- Preventing human immunodeficiency virus type 1 (HIV-1) infection necessitates understanding antibody-mediated virus neutralization.
- The viral envelope glycoprotein (Env) trimer plays a crucial role in HIV-1 infectivity and antibody recognition.
Purpose of the Study:
- To develop a mechanistic model for HIV-1 neutralization incorporating both viral and antibody parameters.
- To define and quantify the antibody perturbation factor (PF) and its impact on neutralization.
Main Methods:
- Development of a mechanistic model for HIV-1 neutralization.
- Inclusion of viral parameters: epitope integrity and Env reactivity.
- Definition and application of the antibody perturbation factor (PF).
Main Results:
- Neutralization susceptibility is influenced by Env trimer integrity and reactivity to antibodies.
- Minimally perturbing (low-PF) antibodies neutralize a broad range of Envs efficiently.
- Highly perturbing (high-PF) antibodies are effective against sensitive Envs, often via irreversible mechanisms.
Conclusions:
- Quantifiable viral and antibody parameters predict HIV-1 neutralization profiles.
- The perturbation factor (PF) is key to understanding antibody potency and mechanism.
- This model advances the prediction of antibody efficacy against diverse HIV-1 strains.
