ArticleThe EMBO journal1995
NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 280 citations in OpenAlex.
- Mucosal T cell activation pathways are upregulated by equine herpesvirus type 1 infection.Veterinary research · 2026Article
- Resolving the cellular profile of germinal center-analogous microstructures in zebrafish.Frontiers in immunology · 2026Article
- Porcine Recombinant NK-Lysin Inhibits the Growth and Metastasis of Murine Hepatocellular Carcinoma In Vivo.Molecules (Basel, Switzerland) · 2025Article
- Piggybacking on nature: exploring the multifaceted world of porcine β-defensins.Veterinary research · 2025Review
- Article
- Effect of Nk-lysin peptides on bacterial growth, MIC, antimicrobial resistance, and viral activities.Animal biotechnology · 2024Article
- Article
- Genomic Variant in NK-Lysin Gene Is Associated with T Lymphocyte Subpopulations in Pigs.Genes · 2022Article
- Expression and biological functions of Ancylostoma ceylanicum saposin-like protein.Parasitology research · 2021Article
- Marine Transcriptomics Analysis for the Identification of New Antimicrobial Peptides.Marine drugs · 2021Article
- Functional Characterization of Porcine NK-Lysin: A Novel Immunomodulator That Regulates Intestinal Inflammatory Response.Molecules (Basel, Switzerland) · 2021Article
- Bovine NK-lysin-derived peptides have bactericidal effects against Mycobacterium avium subspecies paratuberculosis.Veterinary research · 2021Article
- Oral Delivery ofFrontiers in veterinary science · 2021Article
- Bovine fetal mesenchymal stem cells exert antiproliferative effect against mastitis causing pathogen Staphylococcus aureus.Veterinary research · 2019Article
- Antiviral Activity of a Turbot (Marine drugs · 2019Article
- Synthetic bovine NK-lysin-derived peptide (bNK2A) does not require intra-chain disulfide bonds for bactericidal activity.PloS one · 2019Article
- Integrative Transcriptomic and microRNAomic Profiling Reveals Immune Mechanism for the Resilience to Soybean Meal Stress in Fish Gut and Liver.Frontiers in physiology · 2018Article
- The Saposin-Like Protein AplD Displays Pore-Forming Activity and Participates in Defense Against Bacterial Infection During a Multicellular Stage ofFrontiers in cellular and infection microbiology · 2018Article
- Innate Cell-Mediated Cytotoxic Activity of European Sea Bass Leucocytes Against Nodavirus-Infected Cells: A Functional and RNA-seq Study.Scientific reports · 2017Article
- Zebra Fish Lacking Adaptive Immunity Acquire an Antiviral Alert State Characterized by Upregulated Gene Expression of Apoptosis, Multigene Families, and Interferon-Related Genes.Frontiers in immunology · 2017Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A 78 residue antimicrobial, basic peptide, NK-lysin, with three intrachain disulfide bonds was purified from pig small intestine and characterized. A corresponding clone was isolated from a porcine bone marrow cDNA library. The 780 bp DNA sequence had a reading frame of 129 amino acids which corresponded to NK-lysin. The clone was used to show that stimulation with human interleukin-2 induced synthesis of NK-lysin-specific mRNA in a lymphocyte fraction enriched for T and NK cells. Lower levels of mRNA were detected in tissues known to contain T and NK cells, such as small intestine, spleen and colon. Interleukin-2 also induced both proliferation of the lymphocyte fraction and cytolytic function in these cells. Immunostaining showed that NK-lysin was present in cells positive for CD8, CD2 and CD4. NK-lysin showed high anti-bacterial activity against Escherichia coli and Bacillus megaterium and moderate activity against Acinetobacter calcoaceticus and Streptococcus pyogenes. The peptide showed a marked lytic activity against an NK-sensitive mouse tumour cell line, YAC-1, but it did not lyse red blood cells. The amino acid sequence of NK-lysin exhibits 33% identity with a putative human preproprotein, NKG5, of unknown function but derived from a cDNA clone of activated NK cells. We suggest that NK-lysin is a new effector molecule of cytotoxic T and NK cells.
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