ISSN 1814-6090 (Print)
ISSN 2542-1964 (Online)


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Shmakov P. F., Ibrogimova P. K., Svinin A. O. Detection of novel antimicrobial peptides from the skin of anuran amphibians (Anura) through genomic analysis. Current Studies in Herpetology, 2026, vol. 26, iss. 1, pp. 94-98. DOI: 10.18500/1814-6090-2026-26-1-2-94-98, EDN: ZZYIQS

This is an open access article distributed under the terms of Creative Commons Attribution 4.0 International License (CC-BY 4.0).
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Language: 
Russian
Article type: 
Short communication
UDC: 
577.29
EDN: 
ZZYIQS

Detection of novel antimicrobial peptides from the skin of anuran amphibians (Anura) through genomic analysis

Autors: 
Shmakov Pavel F., University of Tyumen (UTMN)
Ibrogimova Polina K., University of Tyumen (UTMN)
Svinin Anton O., FSBEI HE "Mari State University"
Abstract: 

This study presents the results of our searching for antimicrobial peptide genes in the amphibian skin granular glands using next-generation sequencing. Bioinformatic analysis of genomic data from 36 individuals belonging to 10 species of anuran amphibians revealed sequences of esculentin, temporin, ranacyclin, bradykinin (kininogen-1), and bombinin in three amphibian species (Bombina bombina, Rana arvalis, and Pelophylax ridibundus). The amino acid sequences of these peptides showed 87–100% similarity to known sequences of amphibian antimicrobial peptides. The newly identified variants of antimicrobial peptides may possess therapeutic, antibacterial, antiparasitic, and antifungal activities.

Reference: 
  1. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. Journal of Molecular Biology, 1990, vol. 215, iss. 3, pp. 403–410. https://doi.org/10.1016/S0022-2836(05)80360-2
  2. Attoub S., Mechkarska M., Sonnevend A., Radosavljevic G., Jovanovic I., Lukic M. L., Conlon J. M. Esculentin-2CHa: A host-defense peptide with differential cytotoxicity against bacteria, erythrocytes and tumor cells. Peptides, 2013, vol. 39, pp. 95–102. https://doi.org/10.1016/j.peptides.2012.11.004
  3. Bolger A. M., Lohse M., Usadel B. Trimmomatic: A flexible trimmer for Illumina sequence data. Bioinformatics, 2014, vol. 30, iss. 15, pp. 2114–2020. https://doi.org/10.1093/bioinformatics/btu170
  4. Chen B., Zhang Z., Zhang Q., Xu N., Lu T., Wang T., Hong W., Fu Z., Penuelas J., Gillings M., Qian H. Antimicrobial peptides in the global microbiome: Biosynthetic genes and resistance determinants. Environmental Science & Technology, 2023, vol. 57, iss. 20, pp. 7698–7708. https://doi.org/10.1021/acs.est.3c01664
  5. Di Grazia A., Cappiello F., Imanishi A., Mastrofrancesco A., Picardo M., Paus R., Mangoni M. L. The frog skin-derived antimicrobial peptide Esculentin-1a(1-21)NH2 promotes the migration of human HaCaT keratinocytes in an EGF receptor-dependent manner: A novel promoter of human skin wound healing? PLoS ONE, 2015, vol. 10, no. 6, art. e0128663. https://doi.org/10.1371/journal.pone.0128663
  6. Dodds D. R. Antibiotic resistance: A current epilogue. Biochemical Pharmacology, 2017, vol. 134, pp. 139–146. https://doi.org/10.1016/j.bcp.2016.12.005
  7. Kumar S., Stecher G., Li M., Knyaz C., Tamura K. MEGA X: Molecular evolutionary genetics analysis across computing platforms. Molecular Biology and Evolution, 2018, vol. 35, iss. 6, pp. 1547–1549. https://doi.org/10.1093/molbev/msy096
  8. Mangoni M. L., Fiocco D., Mignogna G., Barra D., Simmaco M. Functional characterisation of the 1–18 fragment of esculentin-1b, an antimicrobial peptide from Rana esculenta. Peptides, 2003, vol. 24, no. 11, pp. 1771–1777. https://doi.org/10.1016/j.peptides.2003.07.029
  9. Novković M., Simunić J., Bojović V., Tossi A., Juretić D. DADP: The database of anuran defense peptides. Bioinformatics, 2012, vol. 28, pp. 1406–1407. https://doi.org/10.1093/bioinformatics/bts141
  10. Rollins-Smith L. A. The importance of antimicrobial peptides (AMPs) in amphibian skin defense. Developmental & Comparative Immunology, 2023, vol. 142, art. 104657. https://doi.org/10.1016/j.dci.2023.104657
  11. Saha M., Sarkar A. Review on multiple facets of drug resistance: A rising challenge in the 21st Century. Journal of Xenobiotics, 2021, vol. 11, iss. 4, pp. 197–214. https://doi.org/10.3390/jox11040013
  12. Simmaco M., Mignogna G., Barra D. Antimicrobial peptides from amphibian skin: What do they tell us? Biopolymers, 1998, vol. 47, iss. 6, pp. 435–450. https://doi.org/10.1002/(SICI)1097-0282(1998)47:6<435:AID-BIP3>3.0.CO;2-8
  13. Simmaco M., Mignogna G., Barra D., Bossa F. Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides. Journal of Biological Chemistry, 1994, vol. 269, iss. 16, pp. 11956–11961.
  14. Simmaco M., Mignogna G., Canofeni S., Miele R., Mangoni M. L., Barra, D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. European Journal of Biochemistry, 1996, vol. 242, iss. 3, pp. 788–792. https://doi.org/10.1111/j.1432-1033.1996.0788r.x
  15. Uddin T. M., Chakraborty A. J., Khusro A., Zidan B. R. M., Mitra S., Emran T. B., Dhama K., Ripon M. K. H., Gajdács M., Sahibzada M. U. K., Hossain M. J., Koirala N. Antibiotic resistance in microbes: History, mechanisms, therapeutic strategies and future prospects. Journal of Infection and Public Health, 2021, vol. 14, iss. 12, pp. 1750–1766. https://doi.org/10.1016/j.jiph.2021.10.020
  16. Vasu S., McGahon M. K., Moffett R. C., Curtis T. M., Conlon J. M., Abdel-Wahab Y. H., Flatt P. R. Esculentin-2CHa(1-30) and its analogues: Stability and mechanisms of insulinotropic action. Journal of Endocrinology, 2017, vol. 232, iss. 3, pp. 423–435. https://doi.org/10.1530/JOE-16-0453
  17. Zhang L. J., Gallo R. L. Antimicrobial peptides. Current Biology, 2016, vol. 26, iss. 1, pp. 14–19. https://doi.org/10.1016/j.cub.2015.11.017
  18. Zhou C., Wang Z., Peng X., Liu Y., Lin Y., Zhang Z., Qiu Y., Jin M., Wang R., Kong D. Discovery of two bombinin peptides with antimicrobial and anticancer activities from the skin secretion of Oriental fire-bellied toad, Bombina orientalis. Chemical Biology & Drug Design, 2018, vol. 91, iss. 1, pp. 50–61. https://doi.org/10.1111/cbdd.13055
Received: 
10.03.2025
Accepted: 
02.04.2026
Published: 
30.06.2026