Evidence map›Paper›PMID 26205976›Full record

ArticleMolecular oral microbiology2016

The conserved carboxyl domain of MorC, an inner membrane protein of Aggregatibacter actinomycetemcomitans, is essential for membrane function.

K P Smith, R D Voogt, T Ruiz, K P Mintz

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular oral microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Virulence and Pathogenicity Properties ofPathogens (Basel, Switzerland) · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Bacterial AsmA Proteins Transfer Glycerophospholipids Between MembranesContact (Thousand Oaks (Ventura County, Calif.))
    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 1 institution in 1 country.

K P SmithDepartment of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT, USA.
R D VoogtDepartment of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT, USA.
T RuizDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT, USA.
K P MintzDepartment of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT, USA.
University of Vermont · US

Funding

Environmental Adaptation and Membrane Physiology of an Oral PathogenR01DE018889 · NIDCR · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI MINTZ, KEITH PETER · 2009 to 2013
$1.8M
STRUCTURE OF ORAL BACTERIAL ADHESINSR01DE017474 · NIDCR · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI RUIZ, TERESA · 2008 to 2012
$1.8M
NIDCR NIH HHS R01 DE017474NIDCR NIH HHS R01-DE017474NIDCR NIH HHS R01 DE018889NIDCR NIH HHS R01-DE018889
6 · The paper itself

Abstract

Morphogenesis protein C (MorC) of Aggregatibacter actinomycetemcomitans is important for maintaining the membrane morphology and integrity of the cell envelope of this oral pathogen. The MorC sequence and operon organization were found to be conserved in Gammaproteobacteria, based on a bioinformatic analysis of 435 sequences from representative organisms. Functional conservation of MorC was investigated using an A. actinomycetemcomitans morC mutant as a model system to express MorC homologs from four phylogenetically diverse representatives of the Gammaproteobacteria: Haemophilus influenzae, Escherichia coli, Pseudomonas aeruginosa, and Moraxella catarrhalis. The A. actinomycetemcomitans strains expressing the homologous proteins were assessed for sensitivity to bile salts, leukotoxin secretion, autoaggregation and membrane morphology. MorC from the most closely related organism (H. influenzae) was functionally identical to MorC from A. actinomycetemcomitans. However, the genes from more distantly related organisms restored some but not all A. actinomycetemcomitans mutant phenotypes. In addition, deletion mutagenesis indicated that the most conserved portion of the protein, the C-terminus DUF490 domain, was necessary to maintain the integrity of the membrane. Deletion of the last 10 amino acids of this domain of the A. actinomycetemcomitans MorC protein was sufficient to disrupt membrane stability and leukotoxin secretion. The data suggest that the MorC sequence is functionally conserved across Gammaproteobacteria and the C-terminus of the protein is essential for maintaining membrane physiology.

Indexed as

Aggregatibacter actinomycetemcomitansAmino Acid SequenceBacterial ProteinsBase SequenceBile Acids and SaltsCell MembraneDNA, BacterialExotoxinsGenes, BacterialMembrane ProteinsMicroscopy, Electron, TransmissionProtein DomainsSequence DeletionBacterial ProteinsBile Acids and SaltsDNA, BacterialExotoxinsleukotoxinMembrane ProteinsDUF490membrane morphologyTamBtoxin secretionYtfN

Identifiers

PMID26205976
PMCPMC4712077
OpenAlexW1886733241

What OpenQuestion holds

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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.