ArticleProceedings of the National Academy of Sciences of the United States of America2020
Structural basis of Chikungunya virus inhibition by monoclonal antibodies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
49 citing papers in PubMed, 1 synthesis or guideline pooled it, 70 citations in OpenAlex.
- A bibliometric analysis of vaccine research on Chikungunya virus: contributors, trends, and emerging frontiers.Frontiers in immunology · 2025Pooled it
- Research progress on the role of host factors in Chikungunya virus infection and intervention strategies.Virulence · 2026Review
- Genetic diversity of the Chikungunya virus E2 gene may have implications for the design of vaccines and therapeutic antibodies.Virus genes · 2026Article
- Recent advances in antiviral drugs for Chikungunya virus (CHIKV): Targets, mechanisms, and development strategies.Acta pharmaceutica Sinica. B · 2026Review
- IgG-Bridging-Seeded Synergistic Aggregation of SARS-CoV-2 Spikes Underlies Potent Neutralization by a Low-Affinity Antibody.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- E2 Protein of Chikungunya Virus: A Narrative Review of Its Potential as a Therapeutic Target.Current drug targets · 2026Review
- Immunopathological mechanisms and targeted intervention strategies for chronic chikungunya arthritis: from viral persistence to autoimmunity.Frontiers in immunology · 2026Review
- An ultrapotent human antibody neutralizes all maturation states of Zika virus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- In Silico Characterization of Conserved Epitopes in Alphavirus E2 Proteins: A Promising Approach for Pan-vaccine Design.ACS omega · 2025Article
- Neutralizing antibodies against Chikungunya virus and structural elucidation of their mechanism of action.Nature communications · 2025Article
- Chikungunya virus and other emerging arthritogenic alphaviruses.Nature reviews. Microbiology · 2025Review
- Determinants of human versus mosquito cell entry by the Chikungunya virus envelope proteins.bioRxiv : the preprint server for biology · 2025Article
- Structural elucidation of a unique binding mode by an intact alphavirus human IgG molecule to a quaternary epitope.Nature communications · 2025Article
- Review
- Neutralizing Antibodies: Role in Immune Response and Viral Vector Based Gene Therapy.International journal of molecular sciences · 2025Review
- Highly Potent Neutralizing Nanobodies Acting Against Chikungunya Virus Infection via Inhibiting Multiple Stages of the Viral Life Cycle.International journal of molecular sciences · 2025Article
- Single-chain antibody gene therapy strategy based on high-throughput screening triggers sustained antiviral activity in the body.Journal of virology · 2025Article
- Exploring distinct modes of inter-spike cross-linking for enhanced neutralization by SARS-CoV-2 antibodies.Nature communications · 2024Article
- The neonatal Fc receptor is a cellular receptor for human astrovirus.Nature microbiology · 2024Article
- Antibody-mediated control mechanisms of viral infections.Immunological reviews · 2024Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Chikungunya virus (CHIKV) is an emerging viral pathogen that causes both acute and chronic debilitating arthritis. Here, we describe the functional and structural basis as to how two anti-CHIKV monoclonal antibodies, CHK-124 and CHK-263, potently inhibit CHIKV infection in vitro and in vivo. Our in vitro studies show that CHK-124 and CHK-263 block CHIKV at multiple stages of viral infection. CHK-124 aggregates virus particles and blocks attachment. Also, due to antibody-induced virus aggregation, fusion with endosomes and egress are inhibited. CHK-263 neutralizes CHIKV infection mainly by blocking virus attachment and fusion. To determine the structural basis of neutralization, we generated cryogenic electron microscopy reconstructions of Fab:CHIKV complexes at 4- to 5-Å resolution. CHK-124 binds to the E2 domain B and overlaps with the Mxra8 receptor-binding site. CHK-263 blocks fusion by binding an epitope that spans across E1 and E2 and locks the heterodimer together, likely preventing structural rearrangements required for fusion. These results provide structural insight as to how neutralizing antibody engagement of CHIKV inhibits different stages of the viral life cycle, which could inform vaccine and therapeutic 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.