ArticlePloS one2014
NKLP27: a teleost NK-lysin peptide that modulates immune response, induces degradation of bacterial DNA, and inhibits bacterial and viral infection.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 99 citations in OpenAlex.
- Review
- Molecular Characterization of the Liver-Expressed Antimicrobial Peptide 2 (LEAP2) fromAnimals : an open access journal from MDPI · 2025Article
- Unlocking the potential: Exploring the application of bioactive peptides in aquaculture.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2025Review
- Synthetic Antimicrobial Peptides Fail to Induce Leucocyte Innate Immune Functions but Elicit Opposing Transcriptomic Profiles in European Sea Bass and Gilthead Seabream.Marine drugs · 2024Article
- New insight into the biological activity ofFrontiers in immunology · 2024Article
- Purification and expression of a novel bacteriocin, JUQZ-1, againstFrontiers in microbiology · 2024Article
- A Non-Canonical Teleost NK-Lysin: Antimicrobial Activity via Multiple Mechanisms.International journal of molecular sciences · 2022Article
- Recent Discoveries on Marine Organism Immunomodulatory Activities.Marine drugs · 2022Review
- Severe Natural Outbreak ofInternational journal of molecular sciences · 2022Article
- Antiviral peptides from aquatic organisms: Functionality and potential inhibitory effect on SARS-CoV-2.Aquaculture (Amsterdam, Netherlands) · 2021Review
- Expression analysis of tissue factor pathway inhibitors TFPI-1 and TFPI-2 in Paralichthys olivaceus and antibacterial and anticancer activity of derived peptides.Veterinary research · 2021Article
- Antiviral Activity of a Turbot (Marine drugs · 2019Article
- Substitution of lysine for isoleucine at the center of the nonpolar face of the antimicrobial peptide, piscidin-1, leads to an increase in the rapidity of bactericidal activity and a reduction in toxicity.Infection and drug resistance · 2019Article
- Mudskipper (Boleophthalmus pectinirostris) Hepcidin-1 and Hepcidin-2 Present Different Gene Expression Profile and Antibacterial Activity and Possess Distinct Protective Effect against Edwardsiella tarda Infection.Probiotics and antimicrobial proteins · 2018Article
- Charge-Driven Interaction of Antimicrobial Peptide NK-2 with Phospholipid Membranes.ACS omega · 2017Article
- Innate Cell-Mediated Cytotoxic Activity of European Sea Bass Leucocytes Against Nodavirus-Infected Cells: A Functional and RNA-seq Study.Scientific reports · 2017Article
- Nucleated Teleost Erythrocytes Play an Nk-Lysin- and Autophagy-Dependent Role in Antiviral Immunity.Frontiers in immunology · 2017Article
- Antimicrobial peptide melittin against Xanthomonas oryzae pv. oryzae, the bacterial leaf blight pathogen in rice.Applied microbiology and biotechnology · 2016Article
- The New Antimicrobial Peptide SpHyastatin from the Mud Crab Scylla paramamosain with Multiple Antimicrobial Mechanisms and High Effect on Bacterial Infection.Frontiers in microbiology · 2016Article
- Turbot (Scophthalmus maximus) vs. VHSV (Viral Hemorrhagic Septicemia Virus): A Review.Frontiers in physiology · 2016Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NK-lysin is an antimicrobial protein produced by cytotoxic T lymphocytes and natural killer cells. In this study, we examined the biological property of a peptide, NKLP27, derived from tongue sole (Cynoglossus semilaevis) NK-lysin. NKLP27 is composed of 27 amino acids and shares little sequence identity with known NK-lysin peptides. NKLP27 possesses bactericidal activity against both Gram-negative and Gram-positive bacteria including common aquaculture pathogens. The bactericidal activity of NKLP27 was dependent on the C-terminal five residues, deletion of which dramatically reduced the activity of NKLP27. During its interaction with the target bacterial cells, NKLP27 destroyed cell membrane integrity, penetrated into the cytoplasm, and induced degradation of genomic DNA. In vivo study showed that administration of tongue sole with NKLP27 before bacterial and viral infection significantly reduced pathogen dissemination and replication in tissues. Further study revealed that fish administered with NKLP27 exhibited significantly upregulated expression of the immune genes including those that are known to be involved in antibacterial and antiviral defense. These results indicate that NKLP27 is a novel antimicrobial against bacterial and viral pathogens, and that the observed effect of NKLP27 on bacterial DNA and host gene expression adds new insights to the action mechanism of fish antimicrobial peptides.
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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.