Evidence map›Paper›PMID 24142255›Full record

ArticleJournal of bacteriology2014

Moraxella catarrhalis expresses a cardiolipin synthase that impacts adherence to human epithelial cells.

Sean W Buskirk, Eric R Lafontaine

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. A global perspective on the genomics ofMicrobial genomics · 2025
    Article
  2. The characterization ofMicrobial genomics · 2022
    Article
  3. Review
  4. Loss of a Cardiolipin Synthase inJournal of bacteriology · 2019
    Article
  5. Article
  6. Panel 4: Report of the Microbiology Panel.Otolaryngology--head and neck surgery : official journal of American Academy of Otolaryngology-Head and Neck Surgery · 2017
    Review
  7. 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

2 authors at 1 institution in 1 country.

Sean W BuskirkDepartment of Infectious Diseases, University of Georgia, Athens, Georgia, USA.
Eric R Lafontaine
University of Georgia · US

Funding

PHS HHS AIO51477
6 · The paper itself

Abstract

The major phospholipid constituents of Moraxella catarrhalis membranes are phosphatidylglycerol, phosphatidylethanolamine, and cardiolipin (CL). However, very little is known regarding the synthesis and function of these phospholipids in M. catarrhalis. In this study, we discovered that M. catarrhalis expresses a cardiolipin synthase (CLS), termed MclS, that is responsible for the synthesis of CL within the bacterium. The nucleotide sequence of mclS is highly conserved among M. catarrhalis isolates and is predicted to encode a protein with significant amino acid similarity to the recently characterized YmdC/ClsC protein of Escherichia coli. Isogenic mclS mutant strains were generated in M. catarrhalis isolates O35E, O12E, and McGHS1 and contained no observable levels of CL. Site-directed mutagenesis of a highly conserved HKD motif of MclS also resulted in a CL-deficient strain. Moraxella catarrhalis, which depends on adherence to epithelial cells for colonization of the human host, displays significantly reduced levels of adherence to HEp-2 and A549 cell lines in the mclS mutant strains compared to wild-type bacteria. The reduction in adherence appears to be attributed to the absence of CL. These findings mark the first instance in which a CLS has been related to a virulence-associated trait.

Indexed as

Bacterial AdhesionCardiolipinsCell LineDNA, BacterialDNA Mutational AnalysisEpithelial CellsEscherichia coli ProteinsGene DeletionHepatocytesHumansMembrane ProteinsMolecular Sequence DataMoraxella catarrhalisMutagenesis, Site-DirectedSequence Analysis, DNASequence Homology, Amino AcidCardiolipinscardiolipin synthetaseDNA, BacterialEscherichia coli ProteinsMembrane ProteinsTransferases (Other Substituted Phosphate Groups)

Identifiers

PMID24142255
PMCPMC3911130
OpenAlexW2011908054

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.