ArticleThe Journal of biological chemistry2015
Mechanisms mediating enhanced neutralization efficacy of staphylococcal enterotoxin B by combinations of monoclonal antibodies.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- A highly neutralizing human monoclonal antibody targeting a novel linear epitope on staphylococcal enterotoxin B.Human vaccines & immunotherapeutics · 2024Article
- Direct Mapping of Polyclonal Epitopes in Serum by HDX-MS.Analytical chemistry · 2024Article
- Interaction Between SARS-CoV-2 and Pathogenic Bacteria.Current microbiology · 2023Review
- Dietary supplementation with spray-dried animal plasma improves vaccine protection in aged mice.Frontiers in nutrition · 2023Article
- Article
- An insight into SARS-CoV-2 structure, pathogenesis, target hunting for drug development and vaccine initiatives.RSC medicinal chemistry · 2022Review
- A monoclonal antibody against staphylococcal enterotoxin B superantigen inhibits SARS-CoV-2 entry in vitro.Structure (London, England : 1993) · 2021Article
- Computational Construction of a Single-Chain Bi-Paratopic Antibody Allosterically Inhibiting TCR-Staphylococcal Enterotoxin B Binding.Frontiers in immunology · 2021Article
- Bactericidal fully human single-chain fragment variable antibodies protect mice against methicillin-resistantClinical & translational immunology · 2021Article
- A monoclonal antibody against staphylococcal enterotoxin B superantigen inhibits SARS-CoV-2 entrybioRxiv : the preprint server for biology · 2020Article
- Identification of a unique TCR repertoire, consistent with a superantigen selection process in Children with Multi-system Inflammatory Syndrome.bioRxiv : the preprint server for biology · 2020Article
- Superantigenic character of an insert unique to SARS-CoV-2 spike supported by skewed TCR repertoire in patients with hyperinflammation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Determining the immunological characteristics of a novel human monoclonal antibody developed against staphylococcal enterotoxin B.Human vaccines & immunotherapeutics · 2020Article
- mRNA: A Novel Avenue to Antibody Therapy?Molecular therapy : the journal of the American Society of Gene Therapy · 2019Review
- Evolving concepts in bone infection: redefining "biofilm", "acute vs. chronic osteomyelitis", "the immune proteome" and "local antibiotic therapy".Bone research · 2019Review
- Engineering therapeutic antibodies to combat infectious diseases.Current opinion in chemical engineering · 2018Article
- Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Monoclonal antibodies protect from Staphylococcal Enterotoxin K (SEK) induced toxic shock and sepsis by USA300 Staphylococcus aureus.Virulence · 2017Article
- RBC Adherence of Immune Complexes Containing Botulinum Toxin Improves Neutralization and Macrophage Uptake.Toxins · 2017Article
- Antibodies and superantibodies in patients with chronic rhinosinusitis with nasal polyps.The Journal of allergy and clinical immunology · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Staphylococcal enterotoxin B (SEB) is a superantigen that cross-links the major histocompatibility complex class II and specific V-β chains of the T-cell receptor, thus forming a ternary complex. Developing neutralizing mAb to disrupt the ternary complex and abrogate the resulting toxicity is a major therapeutic challenge because SEB is effective at very low concentrations. We show that combining two SEB-specific mAbs enhances their efficacy, even though one of the two mAbs by itself has no effect on neutralization. Crystallography was employed for fine-mapping conformational epitopes in binary and ternary complexes between SEB and Fab fragments. NMR spectroscopy was used to validate and identify subtle allosteric changes induced by mAbs binding to SEB. The mapping of epitopes established that a combination of different mAbs can enhance efficacy of mAb-mediated protection from SEB induced lethal shock by two different mechanisms: one mAb mixture promoted clearance of the toxin both in vitro and in vivo by FcR-mediated cross-linking and clearance, whereas the other mAb mixture induced subtle allosteric conformational changes in SEB that perturbed formation of the SEB·T-cell receptor·major histocompatibility complex class II trimer. Finally structural information accurately predicted mAb binding to other superantigens that share conformational epitopes with SEB. Fine mapping of conformational epitopes is a powerful tool to establish the mechanism and optimize the action of synergistic mAb combinations.
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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.