ArticleStructure (London, England : 1993)2022
Structural basis for llama nanobody recognition and neutralization of HIV-1 at the CD4-binding site.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Engineering Protein-Based HIV Entry Inhibitors: Advances, Challenges, and Translational Strategies.Biomolecules · 2026Review
- Nanobodies in biomedicine: from molecular characteristics to fabrication and clinical translation.Military Medical Research · 2026Review
- Review
- AntiBMPNN: Structure-Guided Graph Neural Networks for Precision Antibody Engineering.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- J3ExoA: A Novel Anti-HIV Immunotoxin Fusion of Anti-Gp120 J3VHH and PE38 Fragment ofPharmaceuticals (Basel, Switzerland) · 2025Article
- Research Progress on the Application of Neutralizing Nanobodies in the Prevention and Treatment of Viral Infections.Microorganisms · 2025Review
- PET imaging of HIV-1 envelope protein gp120 usingiScience · 2025Article
- Reprogramming human B cells with custom heavy-chain antibodies.Nature biomedical engineering · 2024Article
- AI-based IsAb2.0 for antibody design.Briefings in bioinformatics · 2024Article
- Ultrapotent Broadly Neutralizing Human-llama Bispecific Antibodies against HIV-1.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Broadly neutralizing antibodies targeting HIV: Progress and challenges.Clinical immunology (Orlando, Fla.) · 2023Review
- Identification of two novel neutralizing nanobodies against swine hepatitis E virus.Frontiers in microbiology · 2022Article
- Bispecific antibody CAP256.J3LS targets V2-apex and CD4-binding sites with high breadth and potency.mAbsArticle
Corrections and comments
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Authors and funding
20 authors at 4 institutions in 3 countries.
Funding
Abstract
Nanobodies can achieve remarkable neutralization of genetically diverse pathogens, including HIV-1. To gain insight into their recognition, we determined crystal structures of four llama nanobodies (J3, A12, C8, and D7), all of which targeted the CD4-binding site, in complex with the HIV-1 envelope (Env) gp120 core, and determined a cryoelectron microscopy (cryo-EM) structure of J3 with the Env trimer. Crystal and cryo-EM structures of J3 complexes revealed this nanobody to mimic binding to the prefusion-closed trimer for the primary site of CD4 recognition as well as a secondary quaternary site. In contrast, crystal structures of A12, C8, and D7 with gp120 revealed epitopes that included portions of the gp120 inner domain, inaccessible on the prefusion-closed trimer. Overall, these structures explain the broad and potent neutralization of J3 and limited neutralization of A12, C8, and D7, which utilized binding modes incompatible with the neutralization-targeted prefusion-closed conformation of Env.
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Registered trials
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