Evidence map›Paper›PMID 27997716›Full record

ReviewMolecular microbiology2017

Collagen-like proteins of pathogenic streptococci.

Slawomir Lukomski, Beth A Bachert, Flavia Squeglia, Rita Berisio

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.7field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 67 citations in OpenAlex.

  1. Phylogenomic analysis of the collagen-like BclA proteins inApplied and environmental microbiology · 2026
    Article
  2. Review
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  10. Local Genomic Surveillance of InvasiveInternational journal of molecular sciences · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. The Chemistry and Biology of Collagen Hybridization.Journal of the American Chemical Society · 2023
    Review
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Slawomir LukomskiDepartment of Microbiology, Immunology, and Cell Biology, West Virginia University School of Medicine, Morgantown, WV, 26506, USA.
Beth A BachertDepartment of Microbiology, Immunology, and Cell Biology, West Virginia University School of Medicine, Morgantown, WV, 26506, USA.
Flavia SquegliaInstitute of Biostructures and Bioimaging, National Research Council, Naples, I-80134, Italy.
Rita BerisioInstitute of Biostructures and Bioimaging, National Research Council, Naples, I-80134, Italy.
Institute of Biostructure and Bioimaging · ITWest Virginia University · US

Funding

Sc1 Proteins of S pyogenes: Biology and FunctionR01AI050666 · NIAID · WEST VIRGINIA UNIVERSITY · PI LUKOMSKI, SLAWOMIR · 2002 to 2005
$1.0M
Scl1-mediated immune evasion of the rheumatologenic group A StreptococcusR21AI083683 · NIAID · WEST VIRGINIA UNIVERSITY · PI LUKOMSKI, SLAWOMIR · 2010 to 2011
$404k
NIAID NIH HHS R01 AI050666NIAID NIH HHS R21 AI083683
6 · The paper itself

Abstract

The collagen domain, which is defined by the presence of the Gly-X-Y triplet repeats, is amongst the most versatile and widespread known structures found in proteins from organisms representing all three domains of life. The streptococcal collagen-like (Scl) proteins are widely present in pathogenic streptococci, including Streptococcus pyogenes, S. agalactiae, S. pneumoniae, and S. equi. Experiments and bioinformatic analyses support the hypothesis that all Scl proteins are homotrimeric and cell wall-anchored. These proteins contain the rod-shaped collagenous domain proximal to cell surface, as well as a variety of outermost non-collagenous domains that generally lack predicted functions but can be grouped into one of six clusters based on sequence similarity. The well-characterized Scl1 proteins of S. pyogenes show a dichotomous switch in ligand binding between human tissue and blood environments. In tissue, Scl1 adhesin specifically recognizes the wound microenvironment, promotes adhesion and biofilm formation, decreases bacterial killing by neutrophil extracellular traps, and modulates S. pyogenes virulence. In blood, ligands include components of complement and coagulation-fibrinolytic systems, as well as plasma lipoproteins. In all, the Scl proteins signify a large family of structurally related surface proteins, which contribute to the ability of streptococci to colonize and cause diseases in humans and animals.

Indexed as

Adhesins, BacterialAmino Acid SequenceAnimalsBacterial AdhesionBacterial ProteinsBiofilmsCollagenHumansProtein BindingProtein DomainsStreptococcus agalactiaeStreptococcus pneumoniaeStreptococcus pyogenesVirulence FactorsAdhesins, BacterialBacterial ProteinsCollagenScl1 protein, StreptococcusStreptococcal collagen-like protein A, Streptococcus pyrogenesVirulence Factors

Identifiers

PMID27997716
PMCPMC5344740
OpenAlexW2563842617

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

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.