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

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Published on: September 14, 2014

Structural and immunogenetic signatures guide CD4-mimetic HIV vaccine development.

Daniel L V Bader¹, Claudia T Flynn², Oleksandr Kalyuzhniy³

¹Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, CA 92037, USA; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

|April 17, 2026

Summary

Developing an HIV vaccine requires understanding broadly neutralizing antibodies (bnAbs). This study analyzes V_H1-46 bnAbs, revealing diverse structures and identifying classes that can guide future vaccine design for optimal targeting.

Keywords:

CD4-binding site CD4bs CP: Immunology HIV N276 glycan barrier broadly neutralizing antibody (bnAb)germline-targeting (GT) vaccine design human immunodeficiency virus immunogenetics

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Published on: November 28, 2018

Area of Science:

Immunology
Structural Biology
Vaccine Development

Background:

HIV vaccine strategies aim to elicit broadly neutralizing antibodies (bnAbs) targeting the CD4-binding site.
These bnAbs are often derived from specific immunoglobulin heavy-chain variable genes, including V_H1-2 and V_H1-46.

Purpose of the Study:

To present an integrated analysis of V_H1-46 bnAbs to guide HIV vaccine design.
To characterize the structural and immunogenetic features of V_H1-46 bnAbs.

Main Methods:

In vitro functional studies of V_H1-46 bnAbs.
Cryo-electron microscopy (cryo-EM) of bnAbs complexed with HIV envelope trimers.
Comprehensive structural and immunogenetic analyses.

Main Results:

V_H1-46 bnAbs utilize diverse light-chain variable genes and LCDR3 lengths found in human repertoires.
Unique LCDR3 signatures influence antibody paratope and binding angle.
Three distinct V_H1-46 bnAb classes (1B2530, CH235, and 561) were identified, with the 561 class having two subtypes.

Conclusions:

V_H1-46 bnAbs exhibit significant diversity in their structural and immunogenetic properties.
Tailoring V_H1-46 priming immunogens to specific bnAb classes is crucial for effective vaccine design.
The 561 class of V_H1-46 bnAbs represents a promising target for germline-targeting vaccine strategies.