Evidence map›Paper›PMID 22076158›Full record

ArticlePloS one2011

Characterization of the sortase repertoire in Bacillus anthracis.

Willy Aucher, Sophie Davison, Agnès Fouet

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. 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
0.8field-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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Toxins · 2024
    Review
  4. Review
  5. Review
  6. TheMicroorganisms · 2020
    Review
  7. A new structural class of bacterial thioester domains reveals a slipknot topology.Protein science : a publication of the Protein Society · 2018
    Article
  8. Article
  9. Article
  10. 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

3 authors at 3 institutions in 1 country.

Willy AucherInstitut Pasteur, Unités Toxines et Pathogénie Bactérienne, Pathogénèse des Toxi-infections Bactériennes, Département de Microbiologie, Paris, France.
Sophie Davison
Agnès Fouet
Centre National de la Recherche Scientifique · FRDélégation Paris 5 · FRInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LPXTG proteins, present in most if not all Gram-positive bacteria, are known to be anchored by sortases to the bacterial peptidoglycan. More than one sortase gene is often encoded in a bacterial species, and each sortase is supposed to specifically anchor given LPXTG proteins, depending of the sequence of the C-terminal cell wall sorting signal (cwss), bearing an LPXTG motif or another recognition sequence. B. anthracis possesses three sortase genes. B. anthracis sortase deleted mutant strains are not affected in their virulence. To determine the sortase repertoires, we developed a genetic screen using the property of the gamma phage to lyse bacteria only when its receptor, GamR, an LPXTG protein, is exposed at the surface. We identified 10 proteins that contain a cell wall sorting signal and are covalently anchored to the peptidoglycan. Some chimeric proteins yielded phage lysis in all sortase mutant strains, suggesting that cwss proteins remained surface accessible in absence of their anchoring sortase, probably as a consequence of membrane localization of yet uncleaved precursor proteins. For definite assignment of the sortase repertoires, we consequently relied on a complementary test, using a biochemical approach, namely immunoblot experiments. The sortase anchoring nine of these proteins has thus been determined. The absence of virulence defect of the sortase mutants could be a consequence of the membrane localization of the cwss proteins.

Indexed as

Amino Acid MotifsAminoacyltransferasesAnimalsAnthraxBacillus anthracisBacterial ProteinsBacteriophage lambdaCell WallCysteine EndopeptidasesMembrane ProteinsMiceMutant Chimeric ProteinsMutationPeptide FragmentsPeptidoglycanProtein Sorting SignalsAminoacyltransferasesBacterial ProteinsCysteine EndopeptidasesMembrane ProteinsMutant Chimeric ProteinsPeptide FragmentsPeptidoglycanProtein Sorting Signalssortase A

Identifiers

PMID22076158
PMCPMC3208642
OpenAlexW2023160857

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.