{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,17]],"date-time":"2026-03-17T11:14:44Z","timestamp":1773746084242,"version":"3.50.1"},"reference-count":30,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2021,7,23]],"date-time":"2021-07-23T00:00:00Z","timestamp":1626998400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antibiotics"],"abstract":"<jats:p>Scorpion venom is a mixture of bioactive peptides, among which neurotoxins and antimicrobial peptides serve especially vital functions. Scorpion venom peptides in Buthidae species have been well described, but toxic peptides from non-Buthidae species have been under-investigated. Here, an antimicrobial peptide gene, Ctri9594, was cloned and functionally identified from the venom of the scorpion Chaerilus tricostatus. The precursor nucleotide sequence of Ctri9594 is 199 nt in length, including a 43 nt 5\u2032 UTR, 115 nt 3\u2032 UTR and 210 nt ORF. The ORF encodes 69 amino acid residues, containing a 21 aa signal peptide, 14 aa mature peptide, 3 aa C-terminal posttranslational processing signal and 31 aa propeptide. Multiple sequence alignment and evolutionary analyses show that Ctri9594 is an antimicrobial peptide in scorpion venom. The mature peptide of Ctri9594 was chemically synthesized with a purity greater than 95% and a molecular mass of 1484.4 Da. Minimum inhibitory concentrations (MICs) indicate that the synthesized mature peptide of Ctri9594 has inhibitory activity against Gram-positive bacteria (Bacillus thuringensis, Bacillus subtilis, Staphylococcus aureus and Micrococcus luteus) but not Gram-negative bacteria (Escherichia coli and Pseudomonas aeruginosa) or a fungus (Candida albicans). The antimicrobial mechanism of Ctri9594 is inferred to be related to its amphiphilic \u03b1-helix structure.<\/jats:p>","DOI":"10.3390\/antibiotics10080896","type":"journal-article","created":{"date-parts":[[2021,7,23]],"date-time":"2021-07-23T00:07:40Z","timestamp":1626998860000},"page":"896","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Molecular Cloning and Functional Identification of the Antimicrobial Peptide Gene Ctri9594 from the Venom of the Scorpion Chaerilus tricostatus"],"prefix":"10.3390","volume":"10","author":[{"given":"Dangui","family":"He","sequence":"first","affiliation":[{"name":"Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072, China"},{"name":"State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhijian","family":"Cao","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ruhong","family":"Zhang","sequence":"additional","affiliation":[{"name":"Renmin Hospital of Wuhan University, Wuhan 430200, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wenhua","family":"Li","sequence":"additional","affiliation":[{"name":"Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072, China"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,7,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.toxicon.2020.06.015","article-title":"Biology, venom composition, and scorpionism induced by brazilian scorpion Tityus stigmurus (Thorell, 1876) (Scorpiones: Buthidae): A mini-review","volume":"185","author":"Furtado","year":"2020","journal-title":"Toxicon"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Due\u00f1as-Cuellar, R.A., Santana, C.J.C., Magalh\u00e3es, A.C.M., Pires, O.R., Fontes, W., and Castro, M.S. (2020). Scorpion toxins and ion channels: Potential applications in cancer therapy. Toxins, 12.","DOI":"10.3390\/toxins12050326"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Yacoub, T., Rima, M., Karam, M., and Fajloun, J.S.A.Z. (2020). Antimicrobials from venomous animals: An overview. Molecules, 25.","DOI":"10.3390\/molecules25102402"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0014-5793(00)01384-3","article-title":"Scorpine, an anti-malaria and anti-bacterial agent purified from scorpion venom","volume":"471","author":"Conde","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Schwartz, E.F., Diego-Garcia, E., Rodriguez de la Vega, R.C., and Possani, L.D. (2007). Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones). BMC Genom., 8.","DOI":"10.1186\/1471-2164-8-119"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1007\/s00018-004-4149-1","article-title":"The scorpine family of defensins: Gene structure, alternative polyadenylation and fold recognition","volume":"61","author":"Zhu","year":"2004","journal-title":"Cell Mol. Life Sci."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1080\/15216540500058899","article-title":"Scorpion venom peptides without disulfide bridges","volume":"57","author":"Zeng","year":"2005","journal-title":"IUBMB Life"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.peptides.2003.12.003","article-title":"Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch","volume":"25","author":"Zeng","year":"2004","journal-title":"Peptides"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1006\/bbrc.2001.5472","article-title":"IsCT, a novel cytotoxic linear peptide from scorpion Opisthacanthus madagascariensis","volume":"286","author":"Dai","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1016\/j.jprot.2011.11.029","article-title":"Extreme diversity of scorpion venom peptides and proteins revealed by transcriptomic analysis: Implication for proteome evolution of scorpion venom arsenal","volume":"75","author":"Ma","year":"2012","journal-title":"J. Proteom."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/j.crvi.2008.07.028","article-title":"Observations on the life history of Chaerilus philippinus Louren\u00e7o & Ythier, 2008 (Scorpiones, Chaerilidae) from the Philippines","volume":"331","author":"Ythier","year":"2008","journal-title":"Comptes Rendus Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jprot.2013.06.007","article-title":"Molecular diversity of Chaerilidae venom peptides reveals the dynamic evolution of scorpion venom components from Buthidae to non-Buthidae","volume":"89","author":"He","year":"2013","journal-title":"J. Proteom."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"5220","DOI":"10.1128\/AAC.00369-11","article-title":"Ctriporin, a new anti-methicillin-resistant Staphylococcus aureus peptide from the venom of the scorpion Chaerilus tricostatus","volume":"55","author":"Fan","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.peptides.2012.04.023","article-title":"Identification of a new specific Kv1.3 channel blocker, Ctri9577, from the scorpion Chaerilus tricostatus","volume":"36","author":"Xie","year":"2012","journal-title":"Peptides"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.peptides.2017.03.005","article-title":"Discovery of three toxin peptides with Kv1.3 channel and IL-2 cytokine-inhibiting activities from Non-Buthidae scorpions, Chaerilus tricostatus and Chaerilus tryznai","volume":"91","author":"Ding","year":"2017","journal-title":"Peptides"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1146\/annurev.bi.53.070184.003313","article-title":"Polyprotein gene expression: Generation of diversity of neuroendocrine peptides","volume":"53","author":"Douglass","year":"1984","journal-title":"Annu. Rev. Biochem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.toxicon.2021.04.002","article-title":"Two new cationic \u03b1-helical peptides identified from the venom gland of Liocheles australasiae possess antimicrobial activity against methicillin-resistant staphylococci","volume":"196","author":"Zhao","year":"2021","journal-title":"Toxicon"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Andr\u00e9, S., Raja, Z., Humblot, V., Piesse, C., Foulon, T., Sereno, D., Oury, B., and Ladram, A. (2020). Functional characterization of temporin-SHe, a new broad-spectrum antibacterial and Leishmanicidal temporin-SH paralog from the sahara frog (Pelophylax saharicus). Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21186713"},{"key":"ref_19","first-page":"406","article-title":"The neighbor-joining method: A new method for reconstructing phylogenetic trees","volume":"4","author":"Saitou","year":"1987","journal-title":"Mol. Biol. Evol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"783","DOI":"10.2307\/2408678","article-title":"Confidence limits on phylogenies: An approach using the bootstrap","volume":"39","author":"Felsenstein","year":"1985","journal-title":"Evolution"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1093\/molbev\/msw054","article-title":"MEGA7: Molecular Evolutionary Genetics Analysis version 7.0 for bigger datasets","volume":"33","author":"Kumar","year":"2016","journal-title":"Mol. Biol. Evol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"eaau5480","DOI":"10.1126\/science.aau5480","article-title":"Antimicrobial peptides: Application informed by evolution","volume":"368","author":"Lazzaro","year":"2020","journal-title":"Science"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1016\/S0140-6736(97)80051-7","article-title":"Peptide antibiotics","volume":"349","author":"Hancock","year":"1997","journal-title":"Lancet"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1007\/s10989-020-10075-x","article-title":"A crosstalk on antimicrobial peptides","volume":"27","author":"Borah","year":"2021","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1080\/17460441.2019.1642322","article-title":"Design of alpha-helical antimicrobial peptides with a high selectivity index","volume":"14","year":"2019","journal-title":"Expert Opin. Drug Discov."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3132","DOI":"10.1128\/AAC.00124-10","article-title":"Damage of the bacterial cell envelope by antimicrobial peptides gramicidin S and PGLa as revealed by transmission and scanning electron microscopy","volume":"54","author":"Hartmann","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1016\/j.bbamem.2006.03.021","article-title":"Alpha-helical antimicrobial peptides--using a sequence template to guide structure-activity relationship studies","volume":"1758","author":"Zelezetsky","year":"2006","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"11477","DOI":"10.1038\/s41598-017-11832-7","article-title":"Highly potent antimicrobial modified peptides derived from the Acinetobacter baumannii phage endolysin LysAB2","volume":"7","author":"Peng","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/nrmicro1098","article-title":"Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?","volume":"3","author":"Brogden","year":"2005","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.3389\/fmicb.2018.01159","article-title":"Therapeutic potential of a scorpion venom-derived antimicrobial peptide and its homologs against antibiotic-resistant gram-positive bacteria","volume":"9","author":"Liu","year":"2018","journal-title":"Front. Microbiol."}],"container-title":["Antibiotics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2079-6382\/10\/8\/896\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:33:41Z","timestamp":1760164421000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2079-6382\/10\/8\/896"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7,23]]},"references-count":30,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2021,8]]}},"alternative-id":["antibiotics10080896"],"URL":"https:\/\/doi.org\/10.3390\/antibiotics10080896","relation":{},"ISSN":["2079-6382"],"issn-type":[{"value":"2079-6382","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,7,23]]}}}