Evidence map›Paper›PMID 24637688›Full record

ArticleAntimicrobial agents and chemotherapy2014

A highly active and negatively charged Streptococcus pyogenes lysin with a rare D-alanyl-L-alanine endopeptidase activity protects mice against streptococcal bacteremia.

Rolf Lood, Assaf Raz, Henrik Molina, Chad W Euler, Vincent A Fischetti

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Novel Phage Lysin Abp013 againstAntibiotics (Basel, Switzerland) · 2022
    Article
  12. Review
  13. Article
  14. Phage-Encoded Endolysins.Antibiotics (Basel, Switzerland) · 2021
    Review
  15. Iranian journal of microbiology · 2020
    Article
  16. Article
  17. Biotechnological Potential ofFrontiers in microbiology · 2020
    Review
  18. In Vitro Activity of the Bacteriophage Endolysin HY-133 againstInternational journal of molecular sciences · 2019
    Article
  19. Review
  20. Review
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

5 authors at 1 institution in 1 country.

Rolf LoodLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York, USA.
Assaf RazLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York, USA.
Henrik MolinaProteomics Resource Center, The Rockefeller University, New York, New York, USA.
Chad W EulerLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York, USA.
Vincent A FischettiLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York, USA vaf@rockefeller.edu.
Rockefeller University · US

Funding

PROPERTIES OF STREPTOCOCCAL M PROTEINR37AI011822 · NIAID · ROCKEFELLER UNIVERSITY · PI FISCHETTI, VINCENT A. · 1987 to 2006
$2.7M
PROPERTIES OF STREPTOCOCCAL M PROTEINR01AI011822 · NIAID · ROCKEFELLER UNIVERSITY · PI FISCHETTI, VINCENT A. · 1985 to 2011
$1.7M
NIAID NIH HHS AI11822NIAID NIH HHS R01 AI011822NIAID NIH HHS R37 AI011822
6 · The paper itself

Abstract

Bacteriophage endolysins have shown great efficacy in killing Gram-positive bacteria. PlyC, a group C streptococcal phage lysin, represents the most efficient lysin characterized to date, with a remarkably high specificity against different streptococcal species, including the important pathogen Streptococcus pyogenes. However, PlyC is a unique lysin, in terms of both its high activity and structure (two distinct subunits). We sought to discover and characterize a phage lysin active against S. pyogenes with an endolysin architecture distinct from that of PlyC to determine if it relies on the same mechanism of action as PlyC. In this study, we identified and characterized an endolysin, termed PlyPy (phage lysin from S. pyogenes), from a prophage infecting S. pyogenes. By in silico analysis, PlyPy was found to have a molecular mass of 27.8 kDa and a pI of 4.16. It was active against a majority of group A streptococci and displayed high levels of activity as well as binding specificity against group B and C streptococci, while it was less efficient against other streptococcal species. PlyPy showed the highest activity at neutral pH in the presence of calcium and NaCl. Surprisingly, its activity was not affected by the presence of the group A-specific carbohydrate, while the activity of PlyC was partly inhibited. Additionally, PlyPy was active in vivo and could rescue mice from systemic bacteremia. Finally, we developed a novel method to determine the peptidoglycan bond cleaved by lysins and concluded that PlyPy exhibits a rare d-alanyl-l-alanine endopeptidase activity. PlyPy thus represents the first lysin characterized from Streptococcus pyogenes and has a mechanism of action distinct from that of PlyC.

Indexed as

AlanineAnimalsBacteremiaEndopeptidasesEnzymesFemaleMiceStreptococcal InfectionsStreptococcus PhagesStreptococcus pyogenesAlanineendolysinEndopeptidasesEnzymeslysin, streptococcus bacteriophage

Identifiers

PMID24637688
PMCPMC4068442
OpenAlexW2127308325

What OpenQuestion holds

Textmetadata
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.