ArticleNature communications2024
Engineering immunogens that select for specific mutations in HIV broadly neutralizing antibodies.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Structural determination of the HIV-1 Variable Region 3 epitope of antibody 19b.Journal of virology · 2026Article
- Scientific synergy between prophylactic and therapeutic HIV vaccines-prevention and cure.NPJ vaccines · 2026Article
- Recent advances in HIV-1 envelope-based vaccine designs for guiding broadly neutralizing antibody response.Journal of virology · 2026Review
- Antibody-mediated targeting of SOSIP HIV-1 Env to skin Langerhans cells potentiates humoral responses.EBioMedicine · 2026Article
- Recurrent SARS-CoV-2 Omicron broadly neutralizing humanized antibodies in different single human VProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Germline-somatic residue synergy reshapes antibody encounter-state pathways to enhance HIV-1 recognition.bioRxiv : the preprint server for biology · 2026Article
- Human immunodeficiency virus vaccines: Advances, challenges and future perspectives.World journal of virology · 2026Review
- Advances in Techniques for the Structure and Functional Optimization of Therapeutic Monoclonal Antibodies.Biomedicines · 2025Review
- Rethinking Optimal Immunogens to Face SARS-CoV-2 Evolution Through Vaccination.Influenza and other respiratory viruses · 2025Review
Corrections and comments
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Authors and funding
26 authors.
Funding
Abstract
Vaccine development targeting rapidly evolving pathogens such as HIV-1 requires induction of broadly neutralizing antibodies (bnAbs) with conserved paratopes and mutations, and in some cases, the same Ig-heavy chains. The current trial-and-error search for immunogen modifications that improve selection for specific bnAb mutations is imprecise. Here, to precisely engineer bnAb boosting immunogens, we use molecular dynamics simulations to examine encounter states that form when antibodies collide with the HIV-1 Envelope (Env). By mapping how bnAbs use encounter states to find their bound states, we identify Env mutations predicted to select for specific antibody mutations in two HIV-1 bnAb B cell lineages. The Env mutations encode antibody affinity gains and select for desired antibody mutations in vivo. These results demonstrate proof-of-concept that Env immunogens can be designed to directly select for specific antibody mutations at residue-level precision by vaccination, thus demonstrating the feasibility of sequential bnAb-inducing HIV-1 vaccine design.
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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.