ArticleNature2011
Streptococcal M1 protein constructs a pathological host fibrinogen network.
Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT02533011 (Heparin Binding Protein), which is not on this map. Cited by 74 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Heparin Binding Protein (HBP) in Sepsis for the Prediction of Disease Progression
Who cites it
74 citing papers in PubMed, 122 citations in OpenAlex.
- Dynamic tethering of M protein drives pathological inflammation during group A Streptococcus infections.PLoS pathogens · 2026Article
- Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026Article
- Host-response trajectories in necrotizing fasciitis: host-pathogen interactions, immune evasion, and immunoparalysis.Frontiers in cellular and infection microbiology · 2026Review
- Structural basis for collagen recognition by theeLife · 2025Article
- M1 protein from group ABlood vessels, thrombosis & hemostasis · 2025Article
- Group A Streptococcus interacts with glycosaminoglycans via M proteins to modulate bacterial adherence in vitro.The FEBS journal · 2025Article
- An mRNA vaccine encoding five conserved Group A Streptococcus antigens.Nature communications · 2025Article
- Fibrinogen-binding M-related proteins facilitate the recruitment of plasminogen by Streptococcus pyogenes.Protein science : a publication of the Protein Society · 2025Article
- Global spread of Streptococcus pyogenes A genomics-supported narrative review.FEMS microbiology reviews · 2025Review
- Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024Review
- SIgA structures bound to Streptococcus pyogenes M4 and human CD89 provide insights into host-pathogen interactions.Nature communications · 2023Article
- The Recruitment and Activation of Plasminogen by Bacteria-The Involvement in Chronic Infection Development.International journal of molecular sciences · 2023Review
- 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
- Article
- Distinct Serotypes of Streptococcal M Proteins Mediate Fibrinogen-Dependent Platelet Activation and Proinflammatory Effects.Infection and immunity · 2022Article
- Application of Homology Modeling by Enhanced Profile-Profile Alignment and Flexible-Fitting Simulation to Cryo-EM Based Structure Determination.International journal of molecular sciences · 2022Article
- Streptococcus pyogenes Forms Serotype- and Local Environment-Dependent Interspecies Protein Complexes.mSystems · 2021Article
- Thrombin-Fibrin(ogen) Interactions, Host Defense and Risk of Thrombosis.International journal of molecular sciences · 2021Review
- More than a Pore: Nonlytic Antimicrobial Functions of Complement and Bacterial Strategies for Evasion.Microbiology and molecular biology reviews : MMBR · 2021Review
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
M1 protein, a major virulence factor of the leading invasive strain of group A Streptococcus, is sufficient to induce toxic-shock-like vascular leakage and tissue injury. These events are triggered by the formation of a complex between M1 and fibrinogen that, unlike M1 or fibrinogen alone, leads to neutrophil activation. Here we provide a structural explanation for the pathological properties of the complex formed between streptococcal M1 and human fibrinogen. A conformationally dynamic coiled-coil dimer of M1 was found to organize four fibrinogen molecules into a specific cross-like pattern. This pattern supported the construction of a supramolecular network that was required for neutrophil activation but was distinct from a fibrin clot. Disruption of this network into other supramolecular assemblies was not tolerated. These results have bearing on the pathophysiology of streptococcal toxic shock.
Indexed as
Identifiers
What OpenQuestion holds
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.