ArticleScientific reports2017
Group A Streptococcal M1 Protein Provides Resistance against the Antimicrobial Activity of Histones.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed.
- 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
- Staphylococcus aureus biofilm extracellular DNA neutralizes the antimicrobial activity of histone H3.NPJ biofilms and microbiomes · 2026Article
- Host Proteome Remodeling During Group A Streptococcus Skin Infection.Molecular & cellular proteomics : MCP · 2026Article
- Revisiting the streptococcal M protein: modern perspectives on antibody function, host interactions, and therapeutic targeting.Frontiers in immunology · 2026Review
- Review
- Editor's Choice Platform for identifying human glycan-specific antibodies against bacterial pathogens using synthetic glycan fragments.Glycobiology · 2025Article
- Lysosomal permeabilization by Group AbioRxiv : the preprint server for biology · 2025Article
- Therapeutic Inhibition of Metalloproteases by Tetracyclines During Infection by Multidrug-Resistant Pseudomonas.The Journal of infectious diseases · 2025Article
- The intricate pathogenicity of Group AVirulence · 2024Review
- Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024Review
- Neutrophil extracellular traps in bacterial infections and evasion strategies.Frontiers in immunology · 2024Review
- Detoxification of reactive oxygen species by the hyaluronic acid capsule of group AInfection and immunity · 2023Article
- PplD is a de-N-acetylase of the cell wall linkage unit of streptococcal rhamnopolysaccharides.Nature communications · 2022Article
- Lipid droplets and the host-pathogen dynamic: FATal attraction?The Journal of cell biology · 2021Review
- Review
- Antibiotic Treatment, Mechanisms for Failure, and Adjunctive Therapies for Infections by Group AFrontiers in microbiology · 2021Review
- Playing With Fire: Proinflammatory Virulence Mechanisms of Group AFrontiers in cellular and infection microbiology · 2021Review
- Group A Streptococcus Infection of the Nasopharynx Requires Proinflammatory Signaling through the Interleukin-1 Receptor.Infection and immunity · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
Histones are essential elements of chromatin structure and gene regulation in eukaryotes. An unexpected attribute of these nuclear proteins is their antimicrobial activity. A framework for histone release and function in host defense in vivo was revealed with the discovery of neutrophil extracellular traps, a specialized cell death process in which DNA-based structures containing histones are extruded to ensnare and kill bacteria. Investigating the susceptibility of various Gram-positive pathogens to histones, we found high-level resistance by one leading human pathogen, group A Streptococcus (GAS). A screen of isogenic mutants revealed that the highly surface-expressed M1 protein, a classical GAS virulence factor, was required for high-level histone resistance. Biochemical and microscopic analyses revealed that the N-terminal domain of M1 protein binds and inactivates histones before they reach their cell wall target of action. This finding illustrates a new pathogenic function for this classic GAS virulence factor, and highlights a potential innate immune evasion strategy that may be employed by other bacterial pathogens.
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.