Evidence map›Paper›PMID 20492673›Full record

ArticleMicrobial cell factories2010

High yield expression of an AHL-lactonase from Bacillus sp. B546 in Pichia pastoris and its application to reduce Aeromonas hydrophila mortality in aquaculture.

Ruidong Chen, Zhigang Zhou, Yanan Cao, Yingguo Bai, Bin Yao

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

45 citing papers in PubMed, 119 citations in OpenAlex.

  1. Review
  2. Article
  3. Molecular Aspects of the Functioning of Pathogenic Bacteria Biofilm Based onInternational journal of molecular sciences · 2024
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  9. Novel Quorum Quenching YtnP Lactonase FromFrontiers in microbiology · 2022
    Article
  10. Marine drugs · 2021
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  11. Attenuation ofAntibiotics (Basel, Switzerland) · 2021
    Article
  12. Review
  13. Article
  14. Whole-Genome Sequencing Analysis of Quorum Quenching Bacterial StrainInternational journal of molecular sciences · 2020
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 1 country.

Ruidong ChenKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
Zhigang Zhou
Yanan Cao
Yingguo Bai
Bin Yao
Chinese Academy of Agricultural Sciences · CNFeed Research Institute · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAeromonas hydrophila is a serious pathogen and can cause hemorrhagic septicemia in fish. To control this disease, antibiotics and chemicals are widely used which can consequently result in "superbugs" and chemical accumulation in the food chain. Though vaccine against A. hydrophila is available, its use is limited due to multiple serotypes of this pathogen and problems of safety and efficacy. Another problem with vaccination is the ability to apply it to small fish especially in high numbers. In this study, we tried a new way to attenuate the A. hydrophila infection by using a quorum quenching strategy with a recombinant AHL-lactonase expressed in Pichia pastoris.

resultsThe AHL-lactonase (AiiAB546) from Bacillus sp. B546 was produced extracellularly in P. pastoris with a yield of 3,558.4 +/- 81.3 U/mL in a 3.7-L fermenter when using 3-oxo-C8-HSL as the substrate. After purification with a HiTrap Q Sepharose column, the recombinant homogenous protein showed a band of 33.6 kDa on SDS-PAGE, higher than the calculated molecular mass (28.14 kDa). Deglycosylation of AiiAB546 with Endo H confirmed the occurrence of N-glycosylation. The purified recombinant AiiAB546 showed optimal activity at pH 8.0 and 20 degrees C, exhibited excellent stability at pH 8.0-12.0 and thermal stability at 70 degrees C, was firstly confirmed to be significantly protease-resistant, and had wide substrate specificity. In application test, when co-injected with A. hydrophila in common carp, recombinant AiiAB546 decreased the mortality rate and delayed the mortality time of fish.

conclusionsOur results not only indicate the possibility of mass-production of AHL-lactonase at low cost, but also open up a promising foreground of application of AHL-lactonase in fish to control A. hydrophila disease by regulating its virulence. To our knowledge, this is the first report on heterologous expression of AHL-lactonase in P. pastoris and attenuating A. hydrophila virulence by co-injection with AHL-lactonase.

Indexed as

Microbial ViabilityAeromonas hydrophilaAnimalsBacillusCarboxylic Ester HydrolasesCloning, MolecularFishesGram-Negative Bacterial InfectionsPichiaCarboxylic Ester HydrolasesN-acyl homoserine lactonase

Identifiers

PMID20492673
PMCPMC2881887
OpenAlexW2144555975

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.