Evidence map›Paper›PMID 30381731›Full record

ArticleAsian-Australasian journal of animal sciences2019

Identification of duck liver-expressed antimicrobial peptide 2 and characterization of its bactericidal activity.

Yeojin Hong, Anh Duc Truong, Janggeun Lee, Kyungbaek Lee, Geun-Bae Kim, Kang-Nyeong Heo, Hyun S Lillehoj, Yeong Ho Hong

Open access · goldAbstract read
In one paragraph

Article in Asian-Australasian journal of animal sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. 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

8 authors at 4 institutions in 3 countries.

Yeojin HongDepartment of Animal Science and Technology, Chung-Ang University, Anseong 17546, Korea.
Anh Duc TruongDepartment of Animal Science and Technology, Chung-Ang University, Anseong 17546, Korea.
Janggeun LeeDepartment of Animal Science and Technology, Chung-Ang University, Anseong 17546, Korea.
Kyungbaek LeeDepartment of Animal Science and Technology, Chung-Ang University, Anseong 17546, Korea.
Geun-Bae KimDepartment of Animal Science and Technology, Chung-Ang University, Anseong 17546, Korea.
Kang-Nyeong HeoPoultry Research Institute, National Institute of Animal Science, RDA, Pyeongchang 25342, Korea.
Hyun S LillehojAnimal Biosciences and Biotechnology Laboratory, Agricultural Research Services, United States Department of Agriculture, Beltsville, MD 20705, USA.
Yeong Ho HongDepartment of Animal Science and Technology, Chung-Ang University, Anseong 17546, Korea.
Chung-Ang University · KRAgricultural Research Service · USNational Institute of Animal Science · KRNational Institute of Veterinary Research · VN

Funding

National Research Foundation of Korea 2015R1D1A1A09059345
6 · The paper itself

Abstract

objectiveThis study was conducted to identify duck liver-expressed antimicrobial peptide 2 (LEAP-2) and demonstrate its antimicrobial activity against various pathogens.

methodsTissue samples were collected from 6 to 8-week-old Pekin ducks (Anas platyrhynchos domesticus), total RNA was extracted, and cDNA was synthesized. To confirm the duck LEAP-2 transcript expression levels, quantitative real-time polymerase chain reaction was conducted. Two kinds of peptides (a linear peptide and a disulfide-type peptide) were synthesized to compare the antimicrobial activity. Then, antimicrobial activity assay and fluorescence microscopic analysis were conducted to demonstrate duck LEAP-2 bactericidal activity.

resultsThe duck LEAP-2 peptide sequence showed high identity with those of other avian species (>85%), as well as more than 55% of identity with mammalian sequences. LEAP-2 mRNA was highly expressed in the liver with duodenum next, and then followed by lung, spleen, bursa and jejunum and was the lowest in the muscle. Both of LEAP-2 peptides efficiently killed bacteria, although the disulfide-type LEAP-2 showed more powerful bactericidal activity. Also, gram-positive bacteria was more susceptible to duck LEAP-2 than gram-negative bacteria. Using microscopy, we confirmed that LEAP-2 peptides could kill bacteria by disrupting the bacterial cell envelope.

conclusionDuck LEAP-2 showed its antimicrobial activity against both gram-positive and gram-negative bacteria. Disulfide bonds were important for the powerful killing effect by disrupting the bacterial cell envelope. Therefore, duck LEAP-2 can be used for effective antibiotics alternatives.

Indexed as

Antimicrobial PeptidesDisulfide BondDuckLiver-expressed Antimicrobial Peptide 2 (LEAP-2)Pathogens

Identifiers

PMID30381731
PMCPMC6601062
OpenAlexW2899502508

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.