Evidence map›Paper›PMID 17785473›Full record

ArticleInfection and immunity2007

Enterococcus faecalis constitutes an unusual bacterial model in lysozyme resistance.

Laurent Hébert, Pascal Courtin, Riccardo Torelli, Maurizio Sanguinetti, Marie-Pierre Chapot-Chartier, Yanick Auffray, Abdellah Benachour

Open access · greenAbstract readComparative Study
In one paragraph

Article in Infection and immunity, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

54 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
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  6. The Impact ofPathogens (Basel, Switzerland) · 2024
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  11. Disruption of theJournal of bacteriology · 2022
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  13. Activation of the extracytoplasmic function σ factor σCurrent opinion in microbiology · 2022
    Review
  14. Article
  15. Mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Review
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  19. Article
  20. Structural basis for theThe Journal of biological chemistry · 2020
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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

7 authors at 3 institutions in 2 countries.

Laurent HébertLaboratoire de Microbiologie de l'Environnement, USC INRA 2017, EA956, Université de Caen, 14032 Caen Cedex, France.
Pascal Courtin
Riccardo Torelli
Maurizio Sanguinetti
Marie-Pierre Chapot-Chartier
Yanick Auffray
Abdellah Benachour
Université de Caen Normandie · FRDépartement Génétique Animale · FRUniversità Cattolica del Sacro Cuore · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysozyme is an important and widespread compound of the host constitutive defense system, and it is assumed that Enterococcus faecalis is one of the few bacteria that are almost completely lysozyme resistant. On the basis of the sequence analysis of the whole genome of E. faecalis V583 strain, we identified two genes that are potentially involved in lysozyme resistance, EF_0783 and EF_1843. Protein products of these two genes share significant homology with Staphylococcus aureus peptidoglycan O-acetyltransferase (OatA) and Streptococcus pneumoniae N-acetylglucosamine deacetylase (PgdA), respectively. In order to determine whether EF_0783 and EF_1843 are involved in lysozyme resistance, we constructed their corresponding mutants and a double mutant. The DeltaEF_0783 mutant and DeltaEF_0783 DeltaEF_1843 double mutant were shown to be more sensitive to lysozyme than the parental E. faecalis JH2-2 strain and DeltaEF_1843 mutant were. However, compared to other bacteria, such as Listeria monocytogenes or S. pneumoniae, the tolerance of DeltaEF_0783 and DeltaEF_0783 DeltaEF_1843 mutants towards lysozyme remains very high. Peptidoglycan structure analysis showed that EF_0783 modifies the peptidoglycan by O acetylation of N-acetyl muramic acid, while the EF_1843 deletion has no obvious effect on peptidoglycan structure under the same conditions. Moreover, the EF_0783 and EF_1843 deletions seem to significantly affect the ability of E. faecalis to survive within murine macrophages. In all, while EF_0783 is currently involved in the lysozyme resistance of E. faecalis, peptidoglycan O acetylation and de-N-acetylation are not the main mechanisms conferring high levels of lysozyme resistance to E. faecalis.

Indexed as

Amino Acid SequenceAnimalsAnti-Bacterial AgentsBacterial ProteinsCells, CulturedChromatography, High Pressure LiquidDrug Resistance, BacterialEnterococcus faecalisGene DeletionListeria monocytogenesMacrophages, PeritonealMiceMolecular Sequence DataMuramidasePeptidoglycanSequence Homology, Amino AcidAnti-Bacterial AgentsBacterial ProteinsMuramidasePeptidoglycan

Identifiers

PMID17785473
PMCPMC2168276
OpenAlexW2116859600

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.