ArticlePLoS pathogens2015
Structural and Functional Characterization of Anti-A33 Antibodies Reveal a Potent Cross-Species Orthopoxviruses Neutralizer.
Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 73 citations in OpenAlex.
- An experimentally validated structure-based computational framework for humanisation of anti-orthopoxvirus antibodies.EBioMedicine · 2026Article
- Exploration of the protein and pharmacological landscape of monkeypox virus treatment: from entry point to end point.Molecular diversity · 2026Review
- Discovery and Structural Characterization of a Highly Protective Neutralizing Antibody Targeting the Mpox Virus A35R Protein.MedComm · 2026Article
- The distinct trimeric structure of the immunodominant chlamydial antigen Major Outer Membrane Protein.Nature communications · 2026Article
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- Rational mpox vaccine design: immunogenicity and protective effect of individual and multicomponent proteins in mice.Emerging microbes & infections · 2025Article
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- Emerging strategies for monkeypox: antigen and antibody applications in diagnostics, vaccines, and treatments.Military Medical Research · 2025Review
- Anti-M1R/B6R antibody characterization and bispecific design for enhanced orthopoxvirus protection.EMBO molecular medicine · 2025Article
- A robust comprehensive immunoinformatics approach for designing a potential multi-epitope based vaccine against a reiterated monkeypox virus.Biochemistry and biophysics reports · 2025Article
- Immune Response to MVA-BN Vaccination for Mpox: Current Evidence and Future Directions.Vaccines · 2025Review
- Poxvirus structural biology for application to vaccine design.Trends in immunology · 2025Review
- Bispecific antibodies targeting MPXV A29 and B6 demonstrate efficacy against MPXV infection.Journal of virology · 2025Article
- Monoclonal Antibodies in Light of Mpox Outbreak: Current Research, Therapeutic Targets, and Animal Models.Antibodies (Basel, Switzerland) · 2025Review
- Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R Protein.Viruses · 2025Article
- Article
- Pox-AbDab: the orthopoxvirus antibody database.Frontiers in immunology · 2025Article
- A penta-component mpox mRNA vaccine induces protective immunity in nonhuman primates.Nature communications · 2024Article
- Development of a competitive ELISA based on the LSDV A33 antigen.Virology journal · 2024Article
- Enhanced Immune Responses in Mice by Combining the Mpox Virus B6R-Protein and Aluminum Hydroxide-CpG Vaccine Adjuvants.Vaccines · 2024Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Vaccinia virus A33 is an extracellular enveloped virus (EEV)-specific type II membrane glycoprotein that is essential for efficient EEV formation and long-range viral spread within the host. A33 is a target for neutralizing antibody responses against EEV. In this study, we produced seven murine anti-A33 monoclonal antibodies (MAbs) by immunizing mice with live VACV, followed by boosting with the soluble A33 homodimeric ectodomain. Five A33 specific MAbs were capable of neutralizing EEV in the presence of complement. All MAbs bind to conformational epitopes on A33 but not to linear peptides. To identify the epitopes, we have adetermined the crystal structures of three representative neutralizing MAbs in complex with A33. We have further determined the binding kinetics for each of the three antibodies to wild-type A33, as well as to engineered A33 that contained single alanine substitutions within the epitopes of the three crystallized antibodies. While the Fab of both MAbs A2C7 and A20G2 binds to a single A33 subunit, the Fab from MAb A27D7 binds to both A33 subunits simultaneously. A27D7 binding is resistant to single alanine substitutions within the A33 epitope. A27D7 also demonstrated high-affinity binding with recombinant A33 protein that mimics other orthopoxvirus strains in the A27D7 epitope, such as ectromelia, monkeypox, and cowpox virus, suggesting that A27D7 is a potent cross-neutralizer. Finally, we confirmed that A27D7 protects mice against a lethal challenge with ectromelia virus.
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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.