Increased immunogen valency improves the maturation of vaccine-elicited HIV-1 VRC01-class antibodies
Parul AgrawaliD, Arineh Khechaduri, Kelsey R. Salladay, Anna J. MacCamyiD, Duncan RalphiD, Andrew O. Riker, Andrew B. Stuart, Latha Kallur SiddaramaiahiD, Xiaoying SheniD, Frederick A. Matsen IViD, David C. MontefioriiD, Leonidas StamatatosiD
Abstract
Antibodies belonging to the VRC01-class display broad and potent neutralizing activities and have been isolated from several people living with HIV (PLWH). A member of that class, monoclonal antibody VRC01, was shown to reduce HIV-acquisition in two phase 2b efficacy trials. VRC01-class antibodies are therefore expected to be a key component of an effective HIV-1 vaccine. In contrast to the VRC01-class antibodies that are highly mutated, their unmutated forms do not engage HIV-1 envelope (Env) and do not display neutralizing activities. Hence, specifically modified Env-derived proteins have been designed to engage the unmutated forms of VRC01-class antibodies, and to activate the corresponding naive B cells. Selected heterologous Env must then be used as boost immunogens to guide the proper maturation of these elicited VRC01-class antibodies. Here we examined whether and how the valency of the prime and boost immunogens influences VRC01-class antibody-maturation. Our findings indicate that, indeed the valency of the immunogen affects the maturation of elicited antibody responses by preferentially selecting VRC01-class antibodies that have accumulated somatic mutations present in broadly neutralizing VRC01-class antibodies isolated from PLWH. As a result, antibodies isolated from animals immunized with the higher valency immunogens display broader Env cross-binding properties and improved neutralizing potentials than those isolated from animals immunized with the lower valency immunogens. Our results are relevant to current and upcoming phase 1 clinical trials that evaluate the ability of novel immunogens aiming to elicit cross-reactive VRC01-class antibody responses. AUTHOR SUMMARYPA performed ELISA, B cell sorting, BCR sequencing analysis, oversaw the analysis of all immunochemical assays, interpreted the results and wrote the manuscript; AK processed tissues from immunized animals, performed B cell staining, and generated mAbs; KRS performed BLI and BCR sequencing; AM performed BCR sequencing; DR and FAM performed phylogenetic analysis and contributed to writing the manuscript; AR performed ELISA and processed tissues from immunized animals, ABS expressed and purified recombinant Envs; LKS expressed and purified mVRC01 mAb; XS and DM performed neutralization assays; LS conceived and oversaw the study and wrote the manuscript.
02 /Specification & Classification
Click any tag to browse matching papers- Citations
- 0
- Organism
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Sequential vaccination matures VRC01-class HIV-1 neutralizing antibodies in humans
Tom G. Caniels, Madhu S. Prabhakaran, … Rogier W. Sanders·bioRxiv·Oct 26, 2026
- Characterization of a vaccine-elicited human antibody with sequence homology to VRC01-class antibodies that binds the C1C2 gp120 domain
M. D. Gray, J. Feng, … L. Stamatatos·bioRxiv·Aug 21, 2021
- Maturation of HIV-1 neutralizing antibodies in a germinal center conditional expression mouse model
Ming Tian, Jillian Davis, … Frederick W. Alt·PLoS PathogensPeer-reviewed·Jun 22, 2026
- Structural survey of HIV-1-neutralizing antibodies targeting Env trimer delineates epitope categories and suggests vaccine templates
Gwo‐Yu Chuang, Jing Zhou, … Peter D. Kwong·bioRxiv·May 2, 2018
- Complete functional mapping of infection- and vaccine-elicited antibodies against the fusion peptide of HIV
A. S. Dingens, P. Acharya, … J. D. Bloom·bioRxiv·Apr 24, 2018
- Adjuvants influence the maturation of VRC01-like antibodies during immunization
M. L. Kudsen, P. Agrawal, … L. Stamatatos·bioRxiv·Jun 10, 2022