Evidence map›Paper›PMID 27322675›Full record

ArticlePloS one2016

Cloning and Expression of β-Defensin from Soiny Mullet (Liza haematocheila), with Insights of its Antibacterial Mechanism.

Zhitao Qi, Wei Xu, Fancui Meng, Qihuan Zhang, Chenglung Chen, Rong Shao

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

6 citing papers in PubMed, 20 citations in OpenAlex.

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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

6 authors at 3 institutions in 2 countries.

Zhitao QiKey Laboratory of Biochemistry and Biotechnology of Marine Wetland of Jiangsu Province, Yancheng Institute of Technology, Yancheng, 224051, Jiangsu, China.
Wei XuKey Laboratory of Biochemistry and Biotechnology of Marine Wetland of Jiangsu Province, Yancheng Institute of Technology, Yancheng, 224051, Jiangsu, China.
Fancui MengTianjin Institute of Pharmaceutical Research, Tianjin, 300193, China.
Qihuan ZhangKey Laboratory of Biochemistry and Biotechnology of Marine Wetland of Jiangsu Province, Yancheng Institute of Technology, Yancheng, 224051, Jiangsu, China.
Chenglung ChenDepartment of Chemistry, National Sun Yat-Sen University, Kaohsiung, 80424, Taiwan, ROC.
Rong ShaoKey Laboratory of Biochemistry and Biotechnology of Marine Wetland of Jiangsu Province, Yancheng Institute of Technology, Yancheng, 224051, Jiangsu, China.
Yancheng Institute of Technology · CNNational Sun Yat-sen University · TWTianjin Institute of Pharmaceutical Research (China) · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Beta-defensins are important part of innate immunity of fish, which are the first defense line against invading pathogens. In this study, the β-defensin (Lhβ-defensin) gene was cloned from spleen tissue of soiny mullet (Liza haematocheila). Lhβ-defensin cDNA was 747 bp in length, encoding 63 amino acids. Sequence alignment revealed that Lhβ-defensin contained six conserved cysteine residues and shared 97.5% sequence identities with grouper (Epinephelus coioides) β-defensin. Realtime PCR revealed that Lhβ-defensin was highest expressed in the immune related organs, such as spleen, kidney and gut of healthy fish. Following Streptococcus dysgalactiae infection, Lhβ-defensin was up-regulated in immune related organs, e.g. 17.6-fold in spleen and 10.87-fold in gut at 24 h post infection (hpi). Lhβ-defensin possessed a monomeric structure of a three-stranded anti-parallel β-sheet and an α-helix stabilized by three disulfide bonds formed by Cys30-Cys58, Cys36-Cys52, and Cys40-Cys59. In addition to the experimental work, computer simulation was also carried out to determine the possible conformation of β-defensin and its interaction with palmitoyloleoylphosphatidylglycerol (POPG), a model of bacteria membrane. The Lhβ-defensin was found to form dimeric structure stabilized by the van der Waals contacts of Leu35 and Cys37 in two anti-parallel β1-strands and the cation-π interaction between Tyr32 and Arg54 respectively in the two β1-strands. The most important interactions between β-defensin and membrane are the electrostatic interactions between Arg residues in β-defensin and head group of POPG bilayer as well as hydrogen bond interactions between them. Our results were useful for further understanding the potential mechanism of antimicrobial property of fish β-defensins.

Indexed as

Amino Acid SequenceAnimalsAnti-Bacterial Agentsbeta-DefensinsCloning, MolecularGene Expression RegulationOrgan SpecificityPhylogenyProtein MultimerizationSequence AlignmentSmegmamorphaStreptococcal InfectionsStreptococcusWaterAnti-Bacterial Agentsbeta-DefensinsWater

Identifiers

PMID27322675
PMCPMC4913945
OpenAlexW2471563496

What OpenQuestion holds

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LicenceCC BY
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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.