ArticleProceedings of the National Academy of Sciences of the United States of America2015
Cryo-EM structures elucidate neutralizing mechanisms of anti-chikungunya human monoclonal antibodies with therapeutic activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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Who cites it
39 citing papers in PubMed, 58 citations in OpenAlex.
- Structural and immunogenic characterisation of ChAdOx1 Chik-derived Chikungunya VLPs supports a mechanistic rationale for vaccine-induced protection.Npj viruses · 2026Article
- Chikungunya virus and other emerging arthritogenic alphaviruses.Nature reviews. Microbiology · 2025Review
- Structural elucidation of a unique binding mode by an intact alphavirus human IgG molecule to a quaternary epitope.Nature communications · 2025Article
- Review
- Label-Free Cell-Based Assay for Characterization of Biomolecules and Receptors.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Antibody-mediated control mechanisms of viral infections.Immunological reviews · 2024Review
- Article
- Structural and functional basis of VLDLR receptor usage by Eastern equine encephalitis virus.bioRxiv : the preprint server for biology · 2023Article
- The evolution of chikungunya virus circulating in Indonesia: Sequence analysis of the orf2 gene encoding the viral structural proteins.International microbiology : the official journal of the Spanish Society for Microbiology · 2023Article
- Antiviral neutralizing antibodies: from in vitro to in vivo activity.Nature reviews. Immunology · 2023Review
- Developing a Prototype Pathogen Plan and Research Priorities for the Alphaviruses.The Journal of infectious diseases · 2023Article
- Computational design of N-linked glycans for high throughput epitope profiling.Protein science : a publication of the Protein Society · 2023Article
- Multiple Factors Involved in Bone Damage Caused by Chikungunya Virus Infection.International journal of molecular sciences · 2023Review
- Structural constraints link differences in neutralization potency of human anti-Eastern equine encephalitis virus monoclonal antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Glycoprotein B Antibodies Completely Neutralize EBV Infection of B Cells.Frontiers in immunology · 2022Article
- The Structural Biology of Eastern Equine Encephalitis Virus, an Emerging Viral Threat.Pathogens (Basel, Switzerland) · 2021Review
- Current and prospective computational approaches and challenges for developing COVID-19 vaccines.Advanced drug delivery reviews · 2021Review
- The mechanistic basis of protection by non-neutralizing anti-alphavirus antibodies.Cell reports · 2021Article
- Modeling Immunity with Rosetta: Methods for Antibody and Antigen Design.Biochemistry · 2021Review
- Recent advances in therapeutic applications of neutralizing antibodies for virus infections: an overview.Immunologic research · 2020Review
Corrections and comments
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Authors and funding
14 authors at 6 institutions in 1 country.
Funding
Abstract
Chikungunya virus (CHIKV) is a mosquito-transmitted alphavirus that causes severe acute and chronic disease in humans. Although highly inhibitory murine and human monoclonal antibodies (mAbs) have been generated, the structural basis of their neutralizing activity remains poorly characterized. Here, we determined the cryo-EM structures of chikungunya virus-like particles complexed with antibody fragments (Fab) of two highly protective human mAbs, 4J21 and 5M16, that block virus fusion with host membranes. Both mAbs bind primarily to sites within the A and B domains, as well as to the B domain's β-ribbon connector of the viral glycoprotein E2. The footprints of these antibodies on the viral surface were consistent with results from loss-of-binding studies using an alanine scanning mutagenesis-based epitope mapping approach. The Fab fragments stabilized the position of the B domain relative to the virus, particularly for the complex with 5M16. This finding is consistent with a mechanism of neutralization in which anti-CHIKV mAbs that bridge the A and B domains impede movement of the B domain away from the underlying fusion loop on the E1 glycoprotein and therefore block the requisite pH-dependent fusion of viral and host membranes.
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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.