ArticleNature communications2019
A quantitative Streptococcus pyogenes-human protein-protein interaction map reveals localization of opsonizing antibodies.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 56 citations in OpenAlex.
- Molecular mechanism of complement interference by Streptococcus pyogenes nuclease A.Communications biology · 2026Article
- Molecular basis and therapeutic potential of sortase A inhibitors as new antibiotics against MDR pathogens.Open biology · 2026Review
- Dynamic tethering of M protein drives pathological inflammation during group A Streptococcus infections.PLoS pathogens · 2026Article
- Lysosomal permeabilization by Group AInfection and immunity · 2026Article
- Rapid Proteome-Wide Discovery of Protein-Protein Interactions With ppIRIS.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Neutrophil Extracellular Traps and Complement Pathways: The Missing Links in Acute Rheumatic Fever and Rheumatic Heart Disease Pathogenesis.Journal of cardiovascular translational research · 2026Review
- Revisiting the streptococcal M protein: modern perspectives on antibody function, host interactions, and therapeutic targeting.Frontiers in immunology · 2026Review
- Characterisation of airway inflammation and proteomes associated with cystic fibrosis-related diabetes.ERJ open research · 2025Article
- Dissecting the properties of circulating IgG against streptococcal pathogens through a combined systems antigenomics-serology workflow.Nature communications · 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
- SIgA structures bound to Streptococcus pyogenes M4 and human CD89 provide insights into host-pathogen interactions.Nature communications · 2023Article
- Epidemiological analysis of Group A streptococcus infection diseases among children in Beijing, China under COVID-19 pandemic.BMC pediatrics · 2023Article
- A human monoclonal antibody bivalently binding two different epitopes in streptococcal M protein mediates immune function.EMBO molecular medicine · 2023Article
- Affinity-Purification Combined with Crosslinking Mass Spectrometry for Identification and Structural Modeling of Host-Pathogen Protein-Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Multienzyme deep learning models improve peptide de novo sequencing by mass spectrometry proteomics.PLoS computational biology · 2023Article
- Role of serotype and virulence determinants ofFrontiers in cellular and infection microbiology · 2023Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A fundamental challenge in medical microbiology is to characterize the dynamic protein-protein interaction networks formed at the host-pathogen interface. Here, we generate a quantitative interaction map between the significant human pathogen, Streptococcus pyogenes, and proteins from human saliva and plasma obtained via complementary affinity-purification and bacterial-surface centered enrichment strategies and quantitative mass spectrometry. Perturbation of the network using immunoglobulin protease cleavage, mixtures of different concentrations of saliva and plasma, and different S. pyogenes serotypes and their isogenic mutants, reveals how changing microenvironments alter the interconnectivity of the interaction map. The importance of host immunoglobulins for the interaction with human complement proteins is demonstrated and potential protective epitopes of importance for phagocytosis of S. pyogenes cells are localized. The interaction map confirms several previously described protein-protein interactions; however, it also reveals a multitude of additional interactions, with possible implications for host-pathogen interactions involving other bacterial species.
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