Evidence map›Paper›PMID 25561716›Full record

ArticleJournal of bacteriology2015

A metalloprotease secreted by the type II secretion system links Vibrio cholerae with collagen.

Bo R Park, Ryszard A Zielke, Igor H Wierzbicki, Kristie C Mitchell, Jeffrey H Withey, Aleksandra E Sikora

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2015. 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
3.6field-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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. mBio · 2025
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  6. Article
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Vibrio cholerae Colonization of Soft-Shelled Turtles.Applied and environmental microbiology · 2017
    Article
  13. Review
  14. Article
  15. Iron and zinc exploitation during bacterial pathogenesis.Metallomics : integrated biometal science · 2015
    Review
  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

6 authors at 2 institutions in 1 country.

Bo R ParkDepartment of Pharmaceutical Sciences, College of Pharmacy, Oregon State University, Corvallis, Oregon, USA.
Ryszard A ZielkeDepartment of Pharmaceutical Sciences, College of Pharmacy, Oregon State University, Corvallis, Oregon, USA.
Igor H WierzbickiDepartment of Pharmaceutical Sciences, College of Pharmacy, Oregon State University, Corvallis, Oregon, USA.
Kristie C MitchellDepartment of Immunology and Microbiology, Wayne State University School of Medicine, Detroit, Michigan, USA.
Jeffrey H WitheyDepartment of Immunology and Microbiology, Wayne State University School of Medicine, Detroit, Michigan, USA.
Aleksandra E SikoraDepartment of Pharmaceutical Sciences, College of Pharmacy, Oregon State University, Corvallis, Oregon, USA Aleksandra.Sikora@oregonstate.edu.ORCID http://orcid.org/0000-0001-7977-2596
Oregon State University · USWayne State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vibrio cholerae is autochthonous to various aquatic niches and is the etiological agent of the life-threatening diarrheal disease cholera. The persistence of V. cholerae in natural habitats is a crucial factor in the epidemiology of cholera. In contrast to the well-studied V. cholerae-chitin connection, scarce information is available about the factors employed by the bacteria for the interaction with collagens. Collagens might serve as biologically relevant substrates, because they are the most abundant protein constituents of metazoan tissues and V. cholerae has been identified in association with invertebrate and vertebrate marine animals, as well as in a benthic zone of the ocean where organic matter, including collagens, accumulates. Here, we describe the characterization of the V. cholerae putative collagenase, VchC, encoded by open reading frame VC1650 and belonging to the subfamily M9A peptidases. Our studies demonstrate that VchC is an extracellular collagenase degrading native type I collagen of fish and mammalian origin. Alteration of the predicted catalytic residues coordinating zinc ions completely abolished the protein enzymatic activity but did not affect the translocation of the protease by the type II secretion pathway into the extracellular milieu. We also show that the protease undergoes a maturation process with the aid of a secreted factor(s). Finally, we propose that V. cholerae is a collagenovorous bacterium, as it is able to utilize collagen as a sole nutrient source. This study initiates new lines of investigations aiming to uncover the structural and functional components of the V. cholerae collagen utilization program.

Indexed as

Amino Acid MotifsCollagenGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicMetalloproteasesRecombinant Fusion ProteinsSubstrate SpecificityVibrio choleraeCollagenMetalloproteasesRecombinant Fusion Proteins

Identifiers

PMID25561716
PMCPMC4336349
OpenAlexW2144978781

What OpenQuestion holds

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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.