ArticleEMBO molecular medicine2023
A human monoclonal antibody bivalently binding two different epitopes in streptococcal M protein mediates immune function.
Article in EMBO molecular medicine, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 19 citations in OpenAlex.
- Affinity Enhancement in Discrete Multivalent MegaMolecules.Chembiochem : a European journal of chemical biology · 2026Article
- Human antibodies as emerging drugs for antimicrobial resistance.Trends in immunology · 2026Review
- Revisiting the streptococcal M protein: modern perspectives on antibody function, host interactions, and therapeutic targeting.Frontiers in immunology · 2026Review
- M1 protein from group ABlood vessels, thrombosis & hemostasis · 2025Article
- EPY001, a Novel Monoclonal Antibody AgainstInternational journal of molecular sciences · 2025Article
- Dimeric DNA Aptamers for the Spike Protein of SARS-CoV-2 Derived from a Structured Library with Dual Random Domains.Small methods · 2025Article
- Dissecting the properties of circulating IgG against streptococcal pathogens through a combined systems antigenomics-serology workflow.Nature communications · 2025Article
- Epitope Mapping with Sidewinder: An XL-MS and Structural Modeling Approach.International journal of molecular sciences · 2025Article
- Streptolysin O accelerates the conversion of plasminogen to plasmin.Nature communications · 2024Article
- Article
- Multimodal Mass Spectrometry Identifies a Conserved Protective Epitope inAnalytical chemistry · 2024Article
- The hinge-engineered IgG1-IgG3 hybrid subclass IgGhNature communications · 2024Article
- Pathogen-driven degradation of endogenous and therapeutic antibodies during streptococcal infections.Nature communications · 2023Article
- A human monoclonal antibody bivalently binding two different epitopes in streptococcal M protein mediates immune function.EMBO molecular medicine · 2023Article
- Group A streptococci induce stronger M protein-fibronectin interaction when specific human antibodies are bound.Frontiers in microbiology · 2023Article
- Invasive Streptococcal Infection Can Lead to the Generation of Cross-Strain Opsonic Antibodies.Microbiology spectrum · 2022Article
Corrections and comments
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Authors and funding
15 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Group A streptococci have evolved multiple strategies to evade human antibodies, making it challenging to create effective vaccines or antibody treatments. Here, we have generated antibodies derived from the memory B cells of an individual who had successfully cleared a group A streptococcal infection. The antibodies bind with high affinity in the central region of the surface-bound M protein. Such antibodies are typically non-opsonic. However, one antibody could effectively promote vital immune functions, including phagocytosis and in vivo protection. Remarkably, this antibody primarily interacts through a bivalent dual-Fab cis mode, where the Fabs bind to two distinct epitopes in the M protein. The dual-Fab cis-binding phenomenon is conserved across different groups of M types. In contrast, other antibodies binding with normal single-Fab mode to the same region cannot bypass the M protein's virulent effects. A broadly binding, protective monoclonal antibody could be a candidate for anti-streptococcal therapy. Our findings highlight the concept of dual-Fab cis binding as a means to access conserved, and normally non-opsonic regions, regions for protective antibody targeting.
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