Evidence map›Paper›PMID 20833793›Full record

ArticleApplied and environmental microbiology2010

Insights into the functionality of the putative residues involved in enterocin AS-48 maturation.

Rubén Cebrián, Mercedes Maqueda, José Luis Neira, Eva Valdivia, Manuel Martínez-Bueno, Manuel Montalbán-López

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.8field-weighted citation impact, top 8% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
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  9. Review
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  12. Review
  13. Circular bacteriocins: biosynthesis and mode of action.Applied and environmental microbiology · 2014
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. AS-48 bacteriocin: close to perfection.Cellular and molecular life sciences : CMLS · 2011
    Review
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 2 institutions in 1 country.

Rubén CebriánDepartment of Microbiology, Facultad de Ciencias, Universidad de Granada, Fuentenueva s/n, E-18071 Granada, Spain.
Mercedes Maqueda
José Luis Neira
Eva Valdivia
Manuel Martínez-Bueno
Manuel Montalbán-López
Universidad de Granada · ESUniversitat de Miguel Hernández d'Elx · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AS-48 is a 70-residue, α-helical, cationic bacteriocin produced by Enterococcus faecalis and is very singular in its circular structure and its broad antibacterial spectrum. The AS-48 preprotein consists of an N-terminal signal peptide (SP) (35 residues) followed by a proprotein moiety that undergoes posttranslational modifications to yield the mature and active circular protein. For the study of the specificity of the region of AS-48 that is responsible for maturation, three single mutants have been generated by site-directed mutagenesis in the as-48A structural gene. The substitutions were made just in the residues that are thought to constitute a recognition site for the SP cleavage enzyme (His-1, Met1) and in those involved in circularization (Met1, Trp70). Each derivative was expressed in the enterococcal JH2-2 strain containing the necessary native biosynthetic machinery for enterocin production. The importance of these derivatives in AS-48 processing has been evaluated on the basis of the production and structural characterization of the corresponding derivatives. Notably, only two of them (Trp70Ala and Met1Ala derivatives) could be purified in different forms and amounts and are characterized for their bactericidal activity and secondary structure. We could not detect any production of AS-48 in JH2-2(pAM401-81(His-1Ile)) by using the conventional chromatographic techniques, despite the high efficiency of the culture conditions applied to produce this enterocin. Our results underline the different important roles of the mutated residues in (i) the elimination of the SP, (ii) the production levels and antibacterial activity of the mature proteins, and (iii) protein circularization. Moreover, our findings suggest that His-1 is critically involved in cleavage site recognition, its substitution being responsible for the blockage of processing, thereby hampering the production of the specific protein in the cellular culture supernatant.

Indexed as

Anti-Bacterial AgentsBacteriocin PlasmidsBacteriocinsCulture MediaEnterococcus faecalisGenetic EngineeringIndustrial MicrobiologyMicrobial Sensitivity TestsMutagenesis, Site-DirectedReverse Transcriptase Polymerase Chain ReactionAnti-Bacterial AgentsBacteriocinsCulture Mediaenterocin AS-48, Enterococcus faecalis

Identifiers

PMID20833793
PMCPMC2976261
OpenAlexW2167410536

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.