ArticleThe Journal of experimental medicine2012
Antibody orientation at bacterial surfaces is related to invasive infection.
Article in The Journal of experimental medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.
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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
54 citing papers in PubMed, 1 synthesis or guideline pooled it, 108 citations in OpenAlex.
- Endogenous IgG hypogammaglobulinaemia in critically ill adults with sepsis: systematic review and meta-analysis.Intensive care medicine · 2015Pooled it
- Trial
- Revisiting the streptococcal M protein: modern perspectives on antibody function, host interactions, and therapeutic targeting.Frontiers in immunology · 2026Review
- Host-response trajectories in necrotizing fasciitis: host-pathogen interactions, immune evasion, and immunoparalysis.Frontiers in cellular and infection microbiology · 2026Review
- Phage receptor binding protein and Fc fragment fusion enhances phagocytosis of Y. enterocolitica.AMB Express · 2025Article
- Epitope Mapping with Sidewinder: An XL-MS and Structural Modeling Approach.International journal of molecular sciences · 2025Article
- The intricate pathogenicity of Group AVirulence · 2024Review
- The hinge-engineered IgG1-IgG3 hybrid subclass IgGhNature communications · 2024Article
- Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024Review
- A distinct variant of the SzM protein ofVirulence · 2023Article
- 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
- Role of serotype and virulence determinants ofFrontiers in cellular and infection microbiology · 2023Article
- Group A streptococci induce stronger M protein-fibronectin interaction when specific human antibodies are bound.Frontiers in microbiology · 2023Article
- Current Promising Strategies against Antibiotic-Resistant Bacterial Infections.Antibiotics (Basel, Switzerland) · 2022Review
- Invasive Streptococcal Infection Can Lead to the Generation of Cross-Strain Opsonic Antibodies.Microbiology spectrum · 2022Article
- Article
- Streptococcus pyogenes Forms Serotype- and Local Environment-Dependent Interspecies Protein Complexes.mSystems · 2021Article
- Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.PLoS pathogens · 2021Review
- Structural determination of Streptococcus pyogenes M1 protein interactions with human immunoglobulin G using integrative structural biology.PLoS computational biology · 2021Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several of the most significant bacterial pathogens in humans, including Streptococcus pyogenes, express surface proteins that bind IgG antibodies via their fragment crystallizable (Fc) region, and the dogma is that this protects the bacteria against phagocytic killing in blood. However, analysis of samples from a patient with invasive S. pyogenes infection revealed dramatic differences in the presence and orientation of IgG antibodies at the surface of bacteria from different sites. In the throat, IgG was mostly bound to the bacterial surface via Fc, whereas in the blood IgG was mostly bound via fragment antigen-binding (Fab). In infected and necrotic tissue, the Fc-binding proteins were removed from the bacterial surface. Further investigation showed that efficient bacterial IgGFc-binding occurs only in IgG-poor environments, such as saliva. As a consequence, the bacteria are protected against phagocytic killing, whereas in blood plasma where the concentration of IgG is high, the antibodies preferentially bind via Fab, facilitating opsonization and bacterial killing. IgG-poor environments represent the natural habitat for IgGFc-binding bacteria, and IgGFc-binding proteins may have evolved to execute their function in such environments. The lack of protection in plasma also helps to explain why cases of severe invasive infections with IgGFc-binding bacteria are so rare compared with superficial and uncomplicated infections.
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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.