ReviewAdvances in experimental medicine and biology2011
The nonideal coiled coil of M protein and its multifarious functions in pathogenesis.
Review in Advances in experimental medicine and biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- Host Proteome Remodeling During Group A Streptococcus Skin Infection.Molecular & cellular proteomics : MCP · 2026Article
- Group A Streptococcus interacts with glycosaminoglycans via M proteins to modulate bacterial adherence in vitro.The FEBS journal · 2025Article
- Old Bug-New Challenges After COVID-19 Pandemic: Severe InvasivePathogens (Basel, Switzerland) · 2025Article
- Cathelicidins: Opportunities and Challenges in Skin Therapeutics and Clinical Translation.Antibiotics (Basel, Switzerland) · 2024Review
- Unveiling the impact ofInfection and immunity · 2024Article
- Group A streptococci induce stronger M protein-fibronectin interaction when specific human antibodies are bound.Frontiers in microbiology · 2023Article
- Increase in invasive group A streptococcal infections in Milan, Italy: a genomic and clinical characterization.Frontiers in microbiology · 2023Article
- Complement Evasion Strategies of Human Pathogenic Bacteria.Indian journal of microbiology · 2020Review
- Novel structure of the N-terminal helical domain of BibA, a group B streptococcus immunogenic bacterial adhesin.Acta crystallographica. Section D, Structural biology · 2020Article
- Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcus pyogenes.Journal of structural biology · 2019Article
- Antibodies to the conserved region of the M protein and a streptococcal superantigen cooperatively resolve toxic shock-like syndrome in HLA-humanized mice.Science advances · 2019Article
- The Molecular Basis of Human IgG-Mediated Enhancement of C4b-Binding Protein Recruitment to Group A Streptococcus.Frontiers in immunology · 2019Article
- Contributions of different modules of the plasminogen-binding Streptococcus pyogenes M-protein that mediate its functional dimerization.Journal of structural biology · 2018Article
- Group A streptococcal M protein activates the NLRP3 inflammasome.Nature microbiology · 2017Article
- Group A Streptococcal M1 Protein Provides Resistance against the Antimicrobial Activity of Histones.Scientific reports · 2017Article
- Conserved patterns hidden within group A Streptococcus M protein hypervariability recognize human C4b-binding protein.Nature microbiology · 2016Article
- Coiled-coil destabilizing residues in the group A Streptococcus M1 protein are required for functional interaction.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cationic antimicrobial peptide resistance mechanisms of streptococcal pathogens.Biochimica et biophysica acta · 2015Review
- Mechanisms of group A Streptococcus resistance to reactive oxygen species.FEMS microbiology reviews · 2015Review
- Increased prevalence of group A streptococcus isolates in streptococcal toxic shock syndrome cases in Japan from 2010 to 2012.Epidemiology and infection · 2015Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The M protein is a major virulence factor of Streptococcus pyogenes (group A Streptococcus, GAS). This gram-positive bacterial pathogen is responsible for mild infections, such as pharyngitis, and severe invasive disease, like streptococcal toxic shock syndrome. M protein contributes to GAS virulence in multifarious ways, including blocking deposition of antibodies and complement, helping formation of microcolonies, neutralizing antimicrobial peptides, and triggering a proinflammatory and procoagulatory state. These functions are specified by interactions between M protein and many host components, especially C4BP and fibrinogen. The former interaction is conserved among many antigenically variant M protein types but occurs in a strikingly sequence-independent manner, and the latter is associated in the M1 protein type with severe invasive disease. Remarkably for a protein of such diverse interactions, the M protein has a relatively simple but nonideal α-helical coiled coil sequence. This sequence nonideality is a crucial feature of M protein. Nonideal residues give rise to specific irregularities in its coiled-coil structure, which are essential for interactions with fibrinogen and establishment of a proinflammatory state. In addition, these structural irregularities are reminiscent of those in myosin and tropomyosin, which are targets for crossreactive antibodies in patients suffering from autoimmune sequelae of GAS infection.
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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.