Evidence map›Paper›PMID 22807482›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

X-ray crystal structure of the streptococcal specific phage lysin PlyC.

Sheena McGowan, Ashley M Buckle, Michael S Mitchell, James T Hoopes, D Travis Gallagher, Ryan D Heselpoth, Yang Shen, Cyril F Reboul, Ruby H P Law, Vincent A Fischetti and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
9.4field-weighted citation impact, top 2% 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

59 citing papers in PubMed, 100 citations in OpenAlex.

  1. Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025
    Review
  2. Review
  3. PlyCYU endolysin targetingApplied and environmental microbiology · 2025
    Article
  4. Review
  5. Journal of oral microbiology · 2025
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Structure and host specificity ofScience advances · 2022
    Article
  12. Review
  13. Immunogenicity of Endolysin PlyC.Antibiotics (Basel, Switzerland) · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. 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

12 authors at 5 institutions in 2 countries.

Sheena McGowanDepartment of Biochemistry and Molecular Biology, Monash University, Clayton 3800, Australia.
Ashley M Buckle
Michael S Mitchell
James T Hoopes
D Travis Gallagher
Ryan D Heselpoth
Yang Shen
Cyril F Reboul
Ruby H P Law
Vincent A Fischetti
James C Whisstock
Daniel C Nelson
Monash University · AUNational Institute of Standards and Technology · USUniversity of Maryland, College Park · USRockefeller University · USUniversity of Maryland, Baltimore · 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

Bacteriophages deploy lysins that degrade the bacterial cell wall and facilitate virus egress from the host. When applied exogenously, these enzymes destroy susceptible microbes and, accordingly, have potential as therapeutic agents. The most potent lysin identified to date is PlyC, an enzyme assembled from two components (PlyCA and PlyCB) that is specific for streptococcal species. Here the structure of the PlyC holoenzyme reveals that a single PlyCA moiety is tethered to a ring-shaped assembly of eight PlyCB molecules. Structure-guided mutagenesis reveals that the bacterial cell wall binding is achieved through a cleft on PlyCB. Unexpectedly, our structural data reveal that PlyCA contains a glycoside hydrolase domain in addition to the previously recognized cysteine, histidine-dependent amidohydrolases/peptidases catalytic domain. The presence of eight cell wall-binding domains together with two catalytic domains may explain the extraordinary potency of the PlyC holoenyzme toward target bacteria.

Indexed as

Crystallography, X-RayEnzymesProtein Structure, QuaternaryProtein Structure, TertiaryStreptococcus equiStreptococcus PhagesViral ProteinsEnzymeslysin, streptococcus bacteriophageViral Proteins

Identifiers

PMID22807482
PMCPMC3412044
OpenAlexW2013598528

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.