Evidence map›Paper›PMID 27588686›Full record

ArticlePloS one2016

Cloning, Purification and Characterization of the Collagenase ColA Expressed by Bacillus cereus ATCC 14579.

Carmen M Abfalter, Esther Schönauer, Karthe Ponnuraj, Markus Huemer, Gabriele Gadermaier, Christof Regl, Peter Briza, Fatima Ferreira, Christian G Huber, Hans Brandstetter and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.5field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Inhibition of Collagenase Q1 ofAdvanced therapeutics · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Expression of a New Recombinant Collagenase Protein ofIranian journal of biotechnology · 2019
    Article
  11. 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 2 institutions in 2 countries.

Carmen M AbfalterDepartment of Molecular Biology, Division of Microbiology, Paris-Lodron University of Salzburg, Salzburg, Austria.
Esther SchönauerDepartment of Molecular Biology, Division of Structural Biology, Paris-Lodron University of Salzburg, Salzburg, Austria.
Karthe PonnurajCentre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai, India.
Markus HuemerDepartment of Molecular Biology, Division of Microbiology, Paris-Lodron University of Salzburg, Salzburg, Austria.
Gabriele GadermaierDepartment of Molecular Biology, Division of Allergy and Immunology, Paris-Lodron University of Salzburg, Salzburg, Austria.
Christof ReglDepartment of Molecular Biology, Division of Chemistry and Bioanalytics, Paris-Lodron University of Salzburg, Salzburg, Austria.
Peter BrizaDepartment of Molecular Biology, Division of Allergy and Immunology, Paris-Lodron University of Salzburg, Salzburg, Austria.
Fatima FerreiraDepartment of Molecular Biology, Division of Allergy and Immunology, Paris-Lodron University of Salzburg, Salzburg, Austria.
Christian G HuberDepartment of Molecular Biology, Division of Chemistry and Bioanalytics, Paris-Lodron University of Salzburg, Salzburg, Austria.
Hans BrandstetterDepartment of Molecular Biology, Division of Structural Biology, Paris-Lodron University of Salzburg, Salzburg, Austria.
Gernot PosseltDepartment of Molecular Biology, Division of Microbiology, Paris-Lodron University of Salzburg, Salzburg, Austria.
Silja WesslerDepartment of Molecular Biology, Division of Microbiology, Paris-Lodron University of Salzburg, Salzburg, Austria.
University of Salzburg · ATUniversity of Madras · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial collagenases differ considerably in their structure and functions. The collagenases ColH and ColG from Clostridium histolyticum and ColA expressed by Clostridium perfringens are well-characterized collagenases that cleave triple-helical collagen, which were therefore termed as ´true´ collagenases. ColA from Bacillus cereus (B. cereus) has been added to the collection of true collagenases. However, the molecular characteristics of B. cereus ColA are less understood. In this study, we identified ColA as a secreted true collagenase from B. cereus ATCC 14579, which is transcriptionally controlled by the regulon phospholipase C regulator (PlcR). B. cereus ATCC 14579 ColA was cloned to express recombinant wildtype ColA (ColAwt) and mutated to a proteolytically inactive (ColAE501A) version. Recombinant ColAwt was tested for gelatinolytic and collagenolytic activities and ColAE501A was used for the production of a polyclonal anti-ColA antibody. Comparison of ColAwt activity with homologous proteases in additional strains of B. cereus sensu lato (B. cereus s.l.) and related clostridial collagenases revealed that B. cereus ATCC 14579 ColA is a highly active peptidolytic and collagenolytic protease. These findings could lead to a deeper insight into the function and mechanism of bacterial collagenases which are used in medical and biotechnological applications.

Indexed as

Genes, BacterialAmino Acid SequenceBacillus cereusCloning, MolecularCollagenasesCollagenases

Identifiers

PMID27588686
PMCPMC5010206
OpenAlexW2516611112

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.