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Updated: Jun 29, 2025

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

High affinity mAb infusion can enhance maximum affinity maturation during HIV Env immunization.

Peter Thomas^1,2, Chloe Rees-Spear¹, Sarah Griffith¹

¹Institute of Immunity and Transplantation, Division of Infection and Immunity, University College London, London WC1E 6BT, UK.

|March 29, 2024

Summary

Infusing high-affinity antibodies can suppress most B cell responses but surprisingly enhances affinity maturation in specific B cell populations. This suggests a targeted approach to boost antibody responses against pathogens like HIV.

Keywords:

Immune response Immunology Virology

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Area of Science:

Immunology
Vaccinology
Molecular Biology

Background:

Antigen-specific antibody infusion's effect on germinal center (GC) responses varies with antibody affinity.
Understanding how antibody affinity influences B cell selection is crucial for vaccine development and immunotherapy.

Purpose of the Study:

To investigate if escalating monoclonal antibody (mAb) affinity during immunization enhances B cell affinity maturation.
To determine the impact of CD4 binding-site (CD4bs)-specific mAb infusion on B cell responses to HIV envelope gp120.

Main Methods:

Mice were immunized with HIV envelope gp120.
Mice received infusions of CD4bs-specific monoclonal antibodies (mAbs) with escalating affinity.
Somatic hypermutation (SHM) and B cell affinity were analyzed using high-throughput sequencing of plasma cells.

Main Results:

While most CD4bs-specific B cells showed reduced SHM and affinity, a subset exhibited increased SHM and affinity.
Plasma cells from mAb-infused mice displayed elevated SHM.
Phylogenetic analysis indicated accelerated differentiation in CD4bs-specific plasma cells.

Conclusions:

High-affinity mAb infusion primarily suppresses most competing B cells.
However, it can selectively increase and expedite affinity maturation in specific epitope-targeted B cell populations.
This finding has implications for designing immunotherapies and vaccines.