Evidence map›Paper›PMID 10919766›Full record

ArticleApplied and environmental microbiology2000

Requirement of autolytic activity for bacteriocin-induced lysis.

M C Martínez-Cuesta, J Kok, E Herranz, C Peláez, T Requena, G Buist

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
9.3field-weighted citation impact, top 2% 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

12 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Antimicrobial Activity ofMicroorganisms · 2021
    Article
  3. Gene-Trait Matching and Prevalence of Nisin Tolerance Systems inFrontiers in bioengineering and biotechnology · 2021
    Article
  4. The pneumococcal social network.PLoS pathogens · 2020
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: genetic requirements.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  11. Article
  12. 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 3 institutions in 3 countries.

M C Martínez-CuestaDepartment of Dairy Science and Technology, Instituto del Frío (CSIC), Ciudad Universitaria, Madrid, Spain.
J Kok
E Herranz
C Peláez
T Requena
G Buist
Consejo Superior de Investigaciones Científicas · ESBiotechnology Institute · USUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacteriocin produced by Lactococcus lactis IFPL105 is bactericidal against several Lactococcus and Lactobacillus strains. Addition of the bacteriocin to exponential-growth-phase cells resulted in all cases in bacteriolysis. The bacteriolytic response of the strains was not related to differences in sensitivity to the bacteriocin and was strongly reduced in the presence of autolysin inhibitors (Co(2+) and sodium dodecyl sulfate). When L. lactis MG1363 and its derivative deficient in the production of the major autolysin AcmA (MG1363acmADelta1) were incubated with the bacteriocin, the latter did not lyse and no intracellular proteins were released into the medium. Incubation of cell wall fragments of L. lactis MG1363, or of L. lactis MG1363acmADelta1 to which extracellular AcmA was added, in the presence or absence of the bacteriocin had no effect on the speed of cell wall degradation. This result indicates that the bacteriocin does not degrade cell walls, nor does it directly activate the autolysin AcmA. The autolysin was also responsible for the observed lysis of L. lactis MG1363 cells during incubation with nisin or the mixture of lactococcins A, B, and M. The results presented here show that lysis of L. lactis after addition of the bacteriocins is caused by the resulting cell damage, which promotes uncontrolled degradation of the cell walls by AcmA.

Indexed as

BacteriolysisBacteriocinsCell WallEnzyme ActivationLactobacillusLactococcusLactococcus lactisMuramidaseN-Acetylmuramoyl-L-alanine AmidaseAcmA protein, Lactococcus lactisBacteriocinsMuramidaseN-Acetylmuramoyl-L-alanine Amidase

Identifiers

PMID10919766
PMCPMC92130
OpenAlexW2104883357

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.