دورية أكاديمية
Antibacterial and anticancer activity of two NK-lysin-derived peptides from the Antarctic teleost Trematomus bernacchii.
| العنوان: | Antibacterial and anticancer activity of two NK-lysin-derived peptides from the Antarctic teleost Trematomus bernacchii. |
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| المؤلفون: | Buonocore F; Dept. for Innovation in Biological, Agro-food and Forest systems (DIBAF), University of Tuscia, Largo dell'Università snc, 01100, Viterbo, Italy., Saraceni PR; Dept. for Innovation in Biological, Agro-food and Forest systems (DIBAF), University of Tuscia, Largo dell'Università snc, 01100, Viterbo, Italy; Italian National Agency for New Technologies, Energy and Sustainable Development (ENEA), Division of Health Protection Technologies, 00123, Rome, Italy., Taddei AR; Center of Large Equipments, Section of Electron Microscopy, University of Tuscia, Largo dell'Università Snc, 01100, Viterbo, Italy., Miccoli A; National Research Council, Inst. for Marine Biological Resources and Biotechnology, 60125, Ancona, Italy., Porcelli F; Dept. for Innovation in Biological, Agro-food and Forest systems (DIBAF), University of Tuscia, Largo dell'Università snc, 01100, Viterbo, Italy., Borocci S; Dept. for Innovation in Biological, Agro-food and Forest systems (DIBAF), University of Tuscia, Largo dell'Università snc, 01100, Viterbo, Italy; National Research Council, Inst. for Biological Systems (ISB-CNR) Secondary Office of Rome-Reaction Mechanisms c/o Department of Chemistry, Sapienza University of Rome, P.le A. Moro 5, 00185, Rome, Italy., Gerdol M; Dept. of Life Sciences, University of Trieste, 34127, Trieste, Italy., Bugli F; Dept. of Basic Biotechnological Sciences, Intensive and Perioperative Clinics, Catholic University of the Sacred Heart, Rome, 00168, Italy; Dept. of Laboratory Sciences and Infectious Diseases, A. Gemelli University Hospital Foundation IRCCS, 00168, Rome, Italy., Sanguinetti M; Dept. of Basic Biotechnological Sciences, Intensive and Perioperative Clinics, Catholic University of the Sacred Heart, Rome, 00168, Italy; Dept. of Laboratory Sciences and Infectious Diseases, A. Gemelli University Hospital Foundation IRCCS, 00168, Rome, Italy., Fausto AM; Dept. for Innovation in Biological, Agro-food and Forest systems (DIBAF), University of Tuscia, Largo dell'Università snc, 01100, Viterbo, Italy., Scapigliati G; Dept. for Innovation in Biological, Agro-food and Forest systems (DIBAF), University of Tuscia, Largo dell'Università snc, 01100, Viterbo, Italy., Picchietti S; Dept. for Innovation in Biological, Agro-food and Forest systems (DIBAF), University of Tuscia, Largo dell'Università snc, 01100, Viterbo, Italy. Electronic address: picchietti@unitus.it. |
| المصدر: | Fish & shellfish immunology [Fish Shellfish Immunol] 2023 Nov; Vol. 142, pp. 109099. Date of Electronic Publication: 2023 Sep 19. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Academic Press Country of Publication: England NLM ID: 9505220 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1095-9947 (Electronic) Linking ISSN: 10504648 NLM ISO Abbreviation: Fish Shellfish Immunol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: London ; New York : Academic Press, c1991- |
| مواضيع طبية MeSH: | Fish Proteins*/genetics , Fish Proteins*/chemistry , Perciformes*/genetics , Perciformes*/metabolism, Humans ; Animals ; Antarctic Regions ; Peptides ; Anti-Bacterial Agents/pharmacology ; Proteolipids/genetics ; Proteolipids/chemistry ; Fishes/metabolism ; Mammals/metabolism |
| مستخلص: | The NK-lysin antimicrobial peptide, first identified in mammals, possesses both antibacterial and cytotoxic activity against cancer cell lines. Homologue peptides isolated from different fish species have been examined for their functional characteristics in the last few years. In this study, a NK-lysin transcript was identified in silico from the head kidney transcriptome of the Antarctic teleost Trematomus bernacchii. The corresponding amino acid sequence, slightly longer than NK-lysins of other fish species, contains six cysteine residues that in mammalian counterparts form three disulphide bridges. Real time-PCR analysis indicated its predominant expression in T. bernacchii immune-related organs and tissues, with greatest mRNA abundance detected in gills and spleen. Instead of focusing on the full T. bernacchii derived NK-lysin mature molecule, we selected a 27 amino acid residue peptide (named NKL-WT), corresponding to the potent antibiotic NK-2 sequence found in human NK-lysin. Moreover, we designed a mutant peptide (named NKL-MUT) in which two alanine residues substitute the two cysteines found in the NKL-WT. The two peptides were obtained by solid phase organic synthesis to investigate their functional features. NKL-WT and NKL-MUT displayed antibacterial activity against the human pathogenic bacterium Enterococcus faecalis and the ESKAPE pathogen Acinetobacter baumannii, respectively. Moreover, at the determined Minimum Inhibitory Concentration and Minimum Bactericidal Concentration values against these pathogens, both peptides showed high selectivity as they did not exhibit any haemolytic activity on erythrocytes or cytotoxic activity against mammalian primary cell lines. Finally, the NKL-MUT selectively triggers the killing of the melanoma cell line B16F10 by means of a pro-apoptotic pathway at a concentration range in which no effects were found in normal mammalian cell lines. In conclusion, the two peptides could be considered as promising candidates in the fight against antibiotic resistance and tumour proliferative action, and also be used as innovative adjuvants, either to decrease chemotherapy side effects or to enhance anticancer drug activity. Competing Interests: Declaration of competing interest All authors declare no conflict of interest. (Copyright © 2023 The Authors. Published by Elsevier Ltd.. All rights reserved.) |
| فهرسة مساهمة: | Keywords: Acinetobacter baumannii; Antimicrobial peptides; Enterococcus faecalis; Melanoma cells; NK-lysin; Trematomus bernacchii |
| المشرفين على المادة: | 0 (NK-lysin) 0 (Fish Proteins) 0 (Peptides) 0 (Anti-Bacterial Agents) 0 (Proteolipids) |
| تواريخ الأحداث: | Date Created: 20230921 Date Completed: 20231103 Latest Revision: 20231103 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/j.fsi.2023.109099 |
| PMID: | 37734650 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1095-9947 |
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| DOI: | 10.1016/j.fsi.2023.109099 |