ArticleCell reports2021
Rapid selection of HIV envelopes that bind to neutralizing antibody B cell lineage members with functional improbable mutations.
Article in Cell reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Rapid elicitation of neutralizing Asn332-glycan-independent antibodies to the V3-glycan epitope of HIV-1 Env in nonhuman primates.Nature immunology · 2026Article
- Iterative immunogen optimization to focus immune responses on a conserved, subdominant viral epitope.bioRxiv : the preprint server for biology · 2025Article
- An engineered immunogen activates diverse HIV broadly neutralizing antibody precursors and promotes acquisition of improbable mutations.Science translational medicine · 2025Article
- Engineering immunogens that select for specific mutations in HIV broadly neutralizing antibodies.Nature communications · 2024Article
- Mutation-guided vaccine design: A process for developing boosting immunogens for HIV broadly neutralizing antibody induction.Cell host & microbe · 2024Article
- Structural basis for breadth development in the HIV-1 V3-glycan targeting DH270 antibody clonal lineage.Nature communications · 2023Article
- Identification of CDRH3 loops in the B cell receptor repertoire that can be engaged by candidate immunogens.PLoS pathogens · 2023Article
- Complementary Roles of Antibody Heavy and Light Chain Somatic Hypermutation in Conferring Breadth and Potency to the HIV-1-Specific CAP256-VRC26 bNAb Lineage.Journal of virology · 2022Article
- Analysis of two cooperating antibodies unveils immune pressure imposed on HIV Env to elicit a V3-glycan supersite broadly neutralizing antibody lineage.Frontiers in immunology · 2022Article
- Neutralization Sensitivity of HIV-1 CRF07_BC From an Untreated Patient With a Focus on Evolution Over Time.Frontiers in cellular and infection microbiology · 2022Article
Corrections and comments
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Authors and funding
16 authors at 2 institutions in 1 country.
Funding
Abstract
Elicitation of broadly neutralizing antibodies (bnAbs) by an HIV vaccine will involve priming the immune system to activate antibody precursors, followed by boosting immunizations to select for antibodies with functional features required for neutralization breadth. The higher the number of acquired mutations necessary for function, the more convoluted are the antibody developmental pathways. HIV bnAbs acquire a large number of somatic mutations, but not all mutations are functionally important. In this study, we identify a minimal subset of mutations sufficient for the function of the naturally occurring V3-glycan bnAb DH270.6. Using antibody library screening, candidate envelope immunogens that interact with DH270.6-like antibodies containing this set of key mutations are identified and selected in vitro. Our results demonstrate that less complex B cell evolutionary pathways than those naturally observed exist for the induction of HIV bnAbs by vaccination, and they establish rational approaches to identify boosting candidate immunogens.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.