Evidence map›Paper›PMID 27737668›Full record

ArticleBMC veterinary research2016

Tissue expression and antibacterial activity of host defense peptides in chicken.

Mi Ok Lee, Hyun-Jun Jang, Deivendran Rengaraj, Seo-Yeong Yang, Jae Yong Han, Susan J Lamont, James E Womack

Open access · goldAbstract read
In one paragraph

Article in BMC veterinary research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 63 citations in OpenAlex.

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  7. Protamine cleavage specificity of the avian pathogenFrontiers in veterinary science · 2024
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  14. Effects of ProbioticsThe journal of poultry science · 2020
    Article
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  18. Review
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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

7 authors at 3 institutions in 2 countries.

Mi Ok LeeWCU Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
Hyun-Jun JangWCU Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
Deivendran RengarajWCU Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
Seo-Yeong YangWCU Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
Jae Yong HanWCU Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
Susan J LamontDepartment of Animal Science, Iowa State University, Ames, IA, USA.
James E WomackWCU Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, Seoul, Korea. jwomack@cvm.tamu.edu.
Seoul National University · KRTexas A&M University · USIowa State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHost defence peptides are a diverse group of small, cationic peptides and are important elements of the first line of defense against pathogens in animals. Expression and functional analysis of host defense peptides has been evaluated in chicken but there are no direct, comprehensive comparisons with all gene family and individual genes.

resultsWe examined the expression patterns of all known cathelicidins, β-defensins and NK-lysin in multiple selected tissues from chickens. CATH1 through 3 were predominantly expressed in the bone marrow, whereas CATHB1 was predominant in bursa of Fabricius. The tissue specific pattern of β-defensins generally fell into two groups. β-defensin1-7 expression was predominantly in bone marrow, whereas β-defensin8-10 and β-defensin13 were highly expressed in liver. NK-lysin expression was highest in spleen. We synthesized peptide products of these gene families and analysed their antibacterial efficacy. Most of the host defense peptides showed antibacterial activity against E.coli with dose-dependent efficacy. β-defensin4 and CATH3 displayed the strongest antibacterial activity among all tested chicken HDPs. Microscopic analyses revealed the killing of bacterium by disrupting membranes with peptide treatment.

conclusionsThese results demonstrate dose-dependent antimicrobial effects of chicken HDPs mediated by membrane damage and demonstrate the differential tissue expression pattern of bioactive HDPs in chicken and the relative antimicrobial potency of the peptides they encode.

Indexed as

Gene Expression RegulationAnimalsAnti-Bacterial AgentsAntimicrobial Cationic Peptidesbeta-DefensinsCathelicidinsCell MembraneChickensEscherichia coliGene Expression ProfilingProteolipidsTissue DistributionAnti-Bacterial AgentsAntimicrobial Cationic Peptidesbeta-DefensinsCathelicidinsNK-lysinProteolipidsAntimicrobialChickenHost defence peptides (HDPs)

Identifiers

PMID27737668
PMCPMC5064907
OpenAlexW2531690436

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.