Evidence map›Paper›PMID 21085950›Full record

ArticleApplied microbiology and biotechnology2011

Lytic enzyme discovery through multigenomic sequence analysis in Clostridium perfringens.

Jonathan E Schmitz, Maria Cristina Ossiprandi, Kareem R Rumah, Vincent A Fischetti

Open access · greenAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.8field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Novel Lytic Enzyme of Prophage Origin fromInternational journal of molecular sciences · 2021
    Article
  4. Article
  5. Thermophile Lytic Enzyme Fusion Proteins that TargetAntibiotics (Basel, Switzerland) · 2019
    Article
  6. Characterization of LysBC17, a Lytic Endopeptidase fromAntibiotics (Basel, Switzerland) · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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.

Jonathan E SchmitzLaboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NY 10065, USA. jschmitz@rockefeller.edu
Maria Cristina Ossiprandi
Kareem R Rumah
Vincent A Fischetti
Rockefeller University · USUniversity of Parma · IT

Funding

Weill Cornell/Rockefeller/Sloan-Kettering MST ProgramT32GM007739 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI HSU, KATHARINE C · 1985 to 2023
$51.1M
Isolaton of new phage enzymes to kill B. anthracisR01AI057472 · NIAID · ROCKEFELLER UNIVERSITY · PI FISCHETTI, VINCENT A. · 2004 to 2014
$3.9M
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 AI057472NIAID NIH HHS AI11822NIAID NIH HHS R01 AI011822NIAID NIH HHS R01 AI057472NIAID NIH HHS R37 AI011822NIGMS NIH HHS GM 07739NIGMS NIH HHS T32 GM007739
6 · The paper itself

Abstract

With their ability to lyse Gram-positive bacteria, phage lytic enzymes (or lysins) have received a great deal of attention as novel anti-infective agents. The number of known genes encoding these peptidoglycan hydrolases has increased markedly in recent years, due in large part to advances in DNA sequencing technology. As the genomes of more and more bacterial species/strains are sequenced, lysin-encoding open reading frames (ORFs) can be readily identified in lysogenized prophage regions. In the current study, we sought to assess lysin diversity for the medically relevant pathogen Clostridium perfringens. The sequenced genomes of nine C. perfringens strains were computationally mined for prophage lysins and lysin-like ORFs, revealing several dozen proteins of various enzymatic classes. Of these lysins, a muramidase from strain ATCC 13124 (termed PlyCM) was chosen for recombinant analysis based on its dissimilarity to previously characterized C. perfringens lysins. Following expression and purification, various biochemical properties of PlyCM were determined in vitro, including pH/salt-dependence and temperature stability. The enzyme exhibited activity at low μg/ml concentrations, a typical value for phage lysins. It was active against 23 of 24 strains of C. perfringens tested, with virtually no activity against other clostridial or non-clostridial species. Overall, PlyCM shows potential for development as an enzybiotic agent, demonstrating how expanding genomic databases can serve as rich pools for biotechnologically relevant proteins.

Indexed as

Genome, BacterialAmino Acid SequenceBacteriophagesCloning, MolecularClostridium perfringensCluster AnalysisComputational BiologyEndopeptidasesEnzyme StabilityGene ExpressionHydrogen-Ion ConcentrationMolecular Sequence DataPhylogenyRecombinant ProteinsSequence AnalysisSequence Homology, Amino AcidendolysinEndopeptidasesRecombinant Proteins

Identifiers

PMID21085950
PMCPMC3711215
OpenAlexW2003511260

What OpenQuestion holds

Textmetadata
LicenceTDM
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.