{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T02:06:08Z","timestamp":1793066768424,"version":"4.5.0"},"reference-count":83,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2024,5,11]],"date-time":"2024-05-11T00:00:00Z","timestamp":1715385600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002848","name":"Agencia Nacional de Investigaci\u00f3n y Desarrollo (ANID)","doi-asserted-by":"publisher","award":["1220921"],"award-info":[{"award-number":["1220921"]}],"id":[{"id":"10.13039\/501100002848","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Kunitz-type peptide expression has been described in the venom of snakes of the Viperidae, Elapidae and Colubridae families. This work aimed to identify these peptides in the venom gland transcriptome of the coral snake Micrurus mipartitus. Transcriptomic analysis revealed a high diversity of venom-associated Kunitz serine protease inhibitor proteins (KSPIs). A total of eight copies of KSPIs were predicted and grouped into four distinctive types, including short KSPI, long KSPI, Kunitz\u2013Waprin (Ku-WAP) proteins, and a multi-domain Kunitz-type protein. From these, one short KSPI showed high identity with Micrurus tener and Austrelaps superbus. The long KSPI group exhibited similarity within the Micrurus genus and showed homology with various elapid snakes and even with the colubrid Pantherophis guttatus. A third group suggested the presence of Kunitz domains in addition to a whey-acidic-protein-type four-disulfide core domain. Finally, the fourth group corresponded to a transcript copy with a putative 511 amino acid protein, formerly annotated as KSPI, which UniProt classified as SPINT1. In conclusion, this study showed the diversity of Kunitz-type proteins expressed in the venom gland transcriptome of M. mipartitus.<\/jats:p>","DOI":"10.3390\/toxins16050224","type":"journal-article","created":{"date-parts":[[2024,5,13]],"date-time":"2024-05-13T09:28:25Z","timestamp":1715592505000},"page":"224","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Unveiling Novel Kunitz- and Waprin-Type Toxins in the Micrurus\u00a0mipartitus Coral Snake Venom Gland: An In Silico Transcriptome Analysis"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4768-4919","authenticated-orcid":false,"given":"M\u00f3nica","family":"Saldarriaga-C\u00f3rdoba","sequence":"first","affiliation":[{"name":"Escuela de Medicina Veterinaria, Universidad Bernardo O\u2019Higgins, Santiago 8320000, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-4962-6065","authenticated-orcid":false,"given":"Claudia","family":"Clavero-Le\u00f3n","sequence":"additional","affiliation":[{"name":"Centro de Investigaci\u00f3n en Recursos Naturales y Sustentabilidad (CIRENYS), Universidad Bernardo O\u2019Higgins, Santiago 8320000, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3299-2246","authenticated-orcid":false,"given":"Paola","family":"Rey-Suarez","sequence":"additional","affiliation":[{"name":"Grupo de Investigaci\u00f3n en Toxinolog\u00eda, Alternativas Terap\u00e9uticas y Alimentarias, Facultad de Ciencias Farmac\u00e9uticas y Alimentarias, Universidad de Antioquia, Medell\u00edn 50010, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7956-900X","authenticated-orcid":false,"given":"Vitelbina","family":"Nu\u00f1ez-Rangel","sequence":"additional","affiliation":[{"name":"Grupo de Investigaci\u00f3n en Toxinolog\u00eda, Alternativas Terap\u00e9uticas y Alimentarias, Facultad de Ciencias Farmac\u00e9uticas y Alimentarias, Universidad de Antioquia, Medell\u00edn 50010, Colombia"},{"name":"Escuela de Microbiolog\u00eda, Universidad de Antioquia, Medell\u00edn 50010, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruben","family":"Avenda\u00f1o-Herrera","sequence":"additional","affiliation":[{"name":"Facultad de Ciencias de la Vida & Centro de Investigaci\u00f3n Marina Quintay (CIMARQ), Universidad Andr\u00e9s Bello, Vi\u00f1a del Mar 2531015, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1167-2174","authenticated-orcid":false,"given":"Stefany","family":"Solano-Gonz\u00e1lez","sequence":"additional","affiliation":[{"name":"Laboratorio de Bioinform\u00e1tica Aplicada, Escuela de Ciencias Biol\u00f3gicas, Universidad Nacional, Heredia 86-3000, Costa Rica"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2578-4609","authenticated-orcid":false,"given":"Juan F.","family":"Alzate","sequence":"additional","affiliation":[{"name":"Departamento de Microbiolog\u00eda y Parasitolog\u00eda, Facultad de Medicina, Universidad de Antioquia, Medell\u00edn 50010, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,5,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.toxicon.2020.09.015","article-title":"The first Kunitz-type proteins from a viperid venom that potentiate neuromuscular transmission","volume":"187","author":"Drofenik","year":"2020","journal-title":"Toxicon"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"3470","DOI":"10.1111\/bph.15814","article-title":"A new Kunitz-type snake toxin family associated with an original mode of interaction with the vasopressin 2 receptor","volume":"179","author":"Ciolek","year":"2022","journal-title":"Br. J. Pharmacol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Tasoulis, T., and Isbister, G.K. (2017). A Review and Database of Snake Venom Proteomes. Toxins, 9.","DOI":"10.3390\/toxins9090290"},{"key":"ref_4","first-page":"31","article-title":"The gene structure and evolution of ku-wap-fusin (Kunitz Waprin Fusion Protein), a novel evolutionary intermediate of the Kunitz Serine Protease Inhibitors and Waprins from Sistrurus catenatus (Massasauga Rattlesnake) Venom Glands","volume":"4","author":"Doley","year":"2010","journal-title":"Open Evol. J."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1007\/s00239-020-09959-9","article-title":"Evolutionary aspects of the structural convergence and functional diversification of Kunitz-Domain Inhibitors","volume":"88","author":"Mishra","year":"2020","journal-title":"J. Mol. Evol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"e20200037","DOI":"10.1590\/1678-9199-jvatitd-2020-0037","article-title":"A Kunitz-type peptide from Dendroaspis polylepis venom as a simultaneous inhibitor of serine and cysteine proteases","volume":"26","author":"Kodama","year":"2020","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/S0014-5793(03)00693-8","article-title":"Adaptive evolution in the snake venom Kunitz\/BPTI protein family","volume":"547","author":"Zupunski","year":"2003","journal-title":"FEBS Lett."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Aird, S.D., da Silva, N.J., Qiu, L., Villar-Briones, A., Saddi, V.A., Pires de Campos Telles, M., Grau, M.L., and Mikheyev, A.S. (2017). Coralsnake Venomics: Analyses of Venom Gland transcriptomes and proteomes of six Brazilian Taxa. Toxins, 9.","DOI":"10.3390\/toxins9060187"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1111\/j.1432-1033.1973.tb03069.x","article-title":"The interaction between alpha chymotrypsin and pancreatic trypsin inhibitor (Kunitz inhibitor), Kinetic and thermodynamic properties","volume":"38","author":"Vincent","year":"1973","journal-title":"Eur. J. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1111\/j.1432-1033.1976.tb10870.x","article-title":"Snake venom toxins. Purification and properties of low-molecular-weight polypeptides of Dendroaspis polylepis polylepis (black mamba) venom","volume":"69","author":"Strydom","year":"1976","journal-title":"Eur. J. Biochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/S0041-0101(01)00227-6","article-title":"Primary structures of four trypsin inhibitor E homologs from venom of Dendroaspis angusticeps: Structure-function comparisons with other dendrotoxin homologs","volume":"40","author":"Sigle","year":"2002","journal-title":"Toxicon"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S0041-0101(00)00162-8","article-title":"Twenty years of dendrotoxins","volume":"39","author":"Harvey","year":"2001","journal-title":"Toxicon"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2621","DOI":"10.3390\/toxins5122621","article-title":"Venom down under: Dynamic evolution of Australian elapid snake toxins","volume":"18","author":"Jackson","year":"2013","journal-title":"Toxins"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Junqueira-de-Azevedo, I.L., Campos, P.F., Ching, A.T., and Mackessy, S.P. (2016). Colubrid Venom Composition: An -Omics Perspective. Toxins, 8.","DOI":"10.3390\/toxins8080230"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"4039","DOI":"10.1007\/s00018-008-8573-5","article-title":"Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes","volume":"65","author":"Earl","year":"2008","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Oguiura, N., Sanchez, L., Duarte, P.V., Sulca-L\u00f3pez, M.A., and Machini, M.T. (2023). Past, present, and future of naturally occurring antimicrobials related to snake venoms. Animals, 13.","DOI":"10.3390\/ani13040744"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1042\/BJ20060318","article-title":"Antimicrobial activity of omwaprin, a new member of the waprin family of snake venom proteins","volume":"402","author":"Nair","year":"2007","journal-title":"Biochem. J."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2266","DOI":"10.1093\/gbe\/evw149","article-title":"Trends in the evolution of snake toxins underscored by an integrative omics approach to profile the venom of the Colubrid Phalotris mertensi","volume":"8","author":"Campos","year":"2016","journal-title":"Genome Biol. Evol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2087","DOI":"10.3389\/fimmu.2020.02087","article-title":"A Vaccine based on Kunitz-Type molecule confers protection against fasciola hepatica challenge by inducing IFN-\u03b3 and antibody immune responses through IL-17A production","volume":"11","author":"Silvane","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.jprot.2017.11.019","article-title":"Peptide fingerprinting of the sea anemone Heteractis magnifica mucus revealed neurotoxins, Kunitz-type proteinase inhibitors and a new \u03b2-defensin \u03b1-amylase inhibitor","volume":"173","author":"Sintsova","year":"2018","journal-title":"J. Proteom."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.ijid.2017.10.024","article-title":"Kunitz-type protease inhibitor as a vaccine candidate against schistosomiasis mansoni","volume":"66","author":"Ranasinghe","year":"2018","journal-title":"Int. J. Infect. Dis."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.gene.2012.11.007","article-title":"Snake venom-like waprin from the frog of Ceratophrys calcarata contains antimicrobial function","volume":"514","author":"Liu","year":"2013","journal-title":"Gene"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1093\/molbev\/msh091","article-title":"Assembling an arsenal: Origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences","volume":"21","author":"Fry","year":"2004","journal-title":"Mol. Biol. Evol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1074\/mcp.M700094-MCP200","article-title":"Evolution of an arsenal: Structural and functional diversification of the venom system in the advanced snakes (Caenophidia)","volume":"7","author":"Fry","year":"2008","journal-title":"Mol. Cell. Proteom."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1038\/s41570-022-00393-7","article-title":"The chemistry of snake venom and its medicinal potential","volume":"6","author":"Oliveira","year":"2022","journal-title":"Nat. Rev. Chem."},{"key":"ref_26","unstructured":"Lomonte, B., Calvete, J.J., Fern\u00e1ndez, J., Pla, D., Rey-Su\u00e1rez, P., Sanz, L., Guti\u00e9rrez, J.M., and Sasa, M. (2021). The Biology of the Coralsnakes, Eagle Mountain Publishing."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.jprot.2019.03.014","article-title":"New insights into the phylogeographic distribution of the 3FTx\/PLA2 venom dichotomy across genus Micrurus in South America","volume":"200","author":"Sanz","year":"2019","journal-title":"J. Proteom."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Lomonte, B., Sasa, M., Rey-Su\u00e1rez, P., Bryan, W., and Guti\u00e9rrez, J.M. (2016). Venom of the Coral Snake Micrurus clarki: Proteomic profile, toxicity, immunological cross-neutralization, and characterization of a Three-Finger Toxin. Toxins, 8.","DOI":"10.3390\/toxins8050138"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"100097","DOI":"10.1016\/j.toxcx.2022.100097","article-title":"Proteomic and toxicological analysis of the venom of Micrurus yatesi and its neutralization by an antivenom","volume":"13","author":"Mena","year":"2022","journal-title":"Toxicon"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Sanz, L., Pla, D., P\u00e9rez, A., Rodr\u00edguez, Y., Zavaleta, A., Salas, M., Lomonte, B., and Calvete, J.J. (2016). Venomic analysis of the poorly studied desert Coral Snake, Micrurus tschudii tschudii, supports the 3FTx\/PLA2 dichotomy across Micrurus Venoms. Toxins, 8.","DOI":"10.3390\/toxins8060178"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1016\/j.jprot.2011.09.003","article-title":"Proteomic and biological characterization of the venom of the redtail coral snake, Micrurus mipartitus (Elapidae), from Colombia and Costa Rica","volume":"75","author":"Lomonte","year":"2011","journal-title":"J. Proteom."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.1016\/j.jprot.2011.04.003","article-title":"Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus","volume":"74","author":"Silva","year":"2011","journal-title":"J. Proteom."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Rodr\u00edguez-Vargas, A., Franco-V\u00e1squez, A.M., Bol\u00edvar-Barbosa, J.A., Vega, N., Reyes-Monta\u00f1o, E., Arregu\u00edn-Espinosa, R., Carbajal-Saucedo, A., Angarita-Sierra, T., and Ruiz-G\u00f3mez, F. (2023). Unveiling the venom composition of the Colombian Coral Snakes Micrurus helleri, M. medemi, and M. sangilensis. Toxins, 15.","DOI":"10.3390\/toxins15110622"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"103863","DOI":"10.1016\/j.jprot.2020.103863","article-title":"Functional, proteomic and transcriptomic characterization of the venom from Micrurus browni browni: Identification of the first lethal multimeric neurotoxin in coral snake venom","volume":"225","author":"Lomonte","year":"2020","journal-title":"J. Proteom."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.toxicon.2018.08.003","article-title":"New insights into the proteomic characterization of the coral snake Micrurus pyrrhocryptus venom","volume":"153","author":"Batista","year":"2018","journal-title":"Toxicon"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.jprot.2016.02.006","article-title":"Integrative characterization of the venom of the coral snake Micrurus dumerilii (Elapidae) from Colombia: Proteome, toxicity, and cross-neutralization by antivenom","volume":"136","author":"Lomonte","year":"2016","journal-title":"J. Proteom."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.toxicon.2015.08.016","article-title":"Snake venomics of Micrurus alleni and Micrurus mosquitensis from the Caribbean region of Costa Rica reveals two divergent compositional patterns in New World elapids","volume":"107","author":"Pla","year":"2015","journal-title":"Toxicon"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.jprot.2019.01.007","article-title":"First look into the venom of Roatan Island\u2019s critically endangered coral snake Micrurus ruatanus: Proteomic characterization, toxicity, immunorecognition and neutralization by an antivenom","volume":"198","author":"Lippa","year":"2019","journal-title":"J. Proteom."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1816","DOI":"10.1021\/pr101091a","article-title":"Venomic and antivenomic analyses of the Central American coral snake, Micrurus nigrocinctus (Elapidae)","volume":"10","author":"Angulo","year":"2011","journal-title":"J. Proteome Res."},{"key":"ref_40","unstructured":"Aird, S.D., and da Silva, N.J. (2021). Advances in Coralsnake Biology with an Emphasis on South America, Eagle Mountain Publishing."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Margres, M.J., Aronow, K., Loyacano, J., and Rokyta, D.R. (2013). The venom-gland transcriptome of the eastern coral snake (Micrurus fulvius) reveals high venom complexity in the intragenomic evolution of venoms. BMC Genom., 14.","DOI":"10.1186\/1471-2164-14-531"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/j.biochi.2021.01.003","article-title":"Protein composition and biochemical characterization of venom from Sonoran Coral Snakes (Micruroides euryxanthus)","volume":"182","author":"Strickland","year":"2021","journal-title":"Biochimie"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Hern\u00e1ndez-Altamirano, J.A., Salazar-Valenzuela, D., Medina-Villamizar, E.J., Quirola, D.R., Patel, K., Vaiyapuri, S., Lomonte, B., and Almeida, J.R. (2022). First Insights into the Venom Composition of Two Ecuadorian Coral Snakes. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232314686"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"37054","DOI":"10.1038\/srep37054","article-title":"Strong and widespread action of site-specific positive selection in the snake venom Kunitz\/BPTI protein family","volume":"6","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Munawar, A., Ali, S.A., Akrem, A., and Betzel, C. (2018). Snake Venom Peptides: Tools of Biodiscovery. Toxins, 10.","DOI":"10.3390\/toxins10110474"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Inagaki, H. (2015). Snake Venom Protease Inhibitors: Enhanced Identification, Expanding Biological Function, and Promising Future, Springer.","DOI":"10.1007\/978-94-007-6648-8_16-1"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1111\/bjh.14591","article-title":"Haemotoxic snake venoms: Their functional activity, impact on snakebite victims and pharmaceutical promise","volume":"177","author":"Slagboom","year":"2017","journal-title":"Br. J. Haematol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.biochi.2011.08.003","article-title":"Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms","volume":"94","author":"Earl","year":"2012","journal-title":"Biochimie"},{"key":"ref_49","unstructured":"Fry, B. (2015). Venomous Reptiles and Their Toxins: Evolution, Pathophysiology, and Biodiscovery, Oxford University Press."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1534\/g3.115.020578","article-title":"Post-transcriptional Mechanisms Contribute Little to Phenotypic Variation in Snake Venoms","volume":"5","author":"Rokyta","year":"2015","journal-title":"G3"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1111\/j.1432-1033.1983.tb07481.x","article-title":"Serine proteinase inhibitors from Vipera ammodytes venom. Isolation and kinetic studies","volume":"133","author":"Ritonja","year":"1983","journal-title":"Eur. J. Biochem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/j.peptides.2007.11.013","article-title":"A novel serine protease inhibitor from Bungarus fasciatus venom","volume":"29","author":"Lu","year":"2008","journal-title":"Peptides"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.toxicon.2017.03.011","article-title":"Pathophysiological significance and therapeutic applications of snake venom protease inhibitors","volume":"131","author":"Thakur","year":"2017","journal-title":"Toxicon"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.cbpc.2015.09.009","article-title":"Purification and characterization of tenerplasminin-1, a serine peptidase inhibitor with antiplasmin activity from the coral snake (Micrurus tener tener) venom","volume":"179","author":"Vivas","year":"2016","journal-title":"Comp. Biochem. Physiol. C Toxicol. Pharmacol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1038\/nature10607","article-title":"A heteromeric Texas coral snake toxin targets acid-sensing ion channels to produce pain","volume":"479","author":"Bohlen","year":"2011","journal-title":"Nature"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.jprot.2018.09.006","article-title":"Unlocking the secrets of banded coral snake (Calliophis intestinalis, Malaysia): A venom with proteome novelty, low toxicity and distinct antigenicity","volume":"192","author":"Tan","year":"2019","journal-title":"J. Proteom."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.toxicon.2016.09.008","article-title":"Venoms of Micrurus coral snakes: Evolutionary trends in compositional patterns emerging from proteomic analyses","volume":"122","author":"Lomonte","year":"2016","journal-title":"Toxicon"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"11674","DOI":"10.1038\/s41598-023-37734-5","article-title":"Unveiling underestimated species diversity within the Central American Coralsnake, a medically important complex of venomous taxa","volume":"13","author":"Jowers","year":"2023","journal-title":"Sci. Rep."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"40097","DOI":"10.1074\/jbc.M305322200","article-title":"Identification of a novel family of proteins in snake venoms. Purification and structural characterization of nawaprin from Naja nigricollis snake venom","volume":"278","author":"Torres","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"5687","DOI":"10.1128\/MCB.25.13.5687-5698.2005","article-title":"Hepatocyte growth factor activator inhibitor type 1 (HAI-1) is required for branching morphogenesis in the chorioallantoic placenta","volume":"25","author":"Tanaka","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1023\/A:1023051500010","article-title":"Roles of hepatocyte growth factor (HGF) activator and HGF activator inhibitor in the pericellular activation of HGF\/scatter factor","volume":"22","author":"Kataoka","year":"2003","journal-title":"Cancer Metastasis Rev."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Urra, F.A., and Araya-Maturana, R. (2017). Targeting Metastasis with Snake Toxins: Molecular Mechanisms. Toxins, 9.","DOI":"10.3390\/toxins9120390"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"28726","DOI":"10.2174\/138161207782023775","article-title":"Snake venom components affecting blood coagulation and the vascular system: Structural similarities and marked diversity","volume":"13","author":"Yamazaki","year":"2007","journal-title":"Curr. Pharm. Des."},{"key":"ref_64","first-page":"716","article-title":"Transcriptomics-guided bottom-up and top-down venomics of neonate and adult specimens of the arboreal rear-fanged Brown Treesnake, Boiga irregularis, from Guam","volume":"74","author":"Pla","year":"2018","journal-title":"J. Proteom."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Gioia, M., Ciaccio, C., Calligari, P., De Simone, G., Sbardella, D., Tundo, G., Fasciglione, G.F., Di Masi, A., Di Pierro, D., and Bocedi, A. (2020). Role of proteolytic enzymes in the COVID-19 infection and promising therapeutic approaches. Biochem. Pharmacol., 182.","DOI":"10.1016\/j.bcp.2020.114225"},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Zhang, H., Tian, M., Qi, W., Wu, J., Zheng, H., Guo, G., Zhang, L., Ranasinghe, S.L., McManus, D.P., and Zhang, W. (2021). Bioinformatic comparison of Kunitz protease inhibitors in Echinococcus granulosus sensu stricto and E. multilocularis and the genes expressed in different developmental stages of E. granulosus s.s. BMC Genom., 22.","DOI":"10.1186\/s12864-021-08219-4"},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Bonturi, C.R., Silva Teixeira, A.B., Rocha, V.M., Valente, P.F., Oliveira, J.R., Filho, C.M., Batista, I.F.C., and Oliva, M.L.V. (2022). Plant Kunitz Inhibitors and their interaction with proteases: Current and potential pharmacological targets. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23094742"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Fratini, E., Rossi, M.N., Spagoni, L., Riccieri, A., Mancini, E., Polticelli, F., Bologna, M.A., Mariottini, P., and Cervelli, M. (2022). Molecular characterization of Kunitz-Type protease inhibitors from Blister Beetles (Coleoptera, Meloidae). Biomolecules, 12.","DOI":"10.3390\/biom12070988"},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Kleiz-Ferreira, J.M., Bernaerts, H., Pinheiro-Junior, E.L., Peigneur, S., Zingali, R.B., and Tytgat, J. (2022). Pharmacological screening of venoms from five Brazilian Micrurus species on different ion channels. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23147714"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"7154","DOI":"10.1073\/pnas.1620454114","article-title":"Green mamba peptide targets type-2 vasopressin receptor against polycystic kidney disease","volume":"114","author":"Ciolek","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Morjen, M., Moslah, W., Touihri-Baraketi, I., Srairi-Abid, N., Luis, J., Marrakchi, N., and Jebali, J. (2022). Expression of the first recombinant anti-tumoral snake venom Kunitz-Type Serine Protease Inhibitor. Toxins, 14.","DOI":"10.3390\/toxins14030170"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2498","DOI":"10.3389\/fimmu.2019.02498","article-title":"Peptides derived of Kunitz-Type Serine Protease Inhibitor as potential vaccine against experimental Schistosomiasis","volume":"10","author":"Protasio","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"10","DOI":"10.14806\/ej.17.1.200","article-title":"Cutadapt removes adapter sequences from high-throughput sequencing reads","volume":"17","author":"Martin","year":"2011","journal-title":"EMBnet. J."},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Rokyta, D.R., Lemmon, A.R., Margres, M.J., and Aronow, K. (2012). The venom-gland transcriptome of the eastern diamondback rattlesnake (Crotalus adamanteus). BMC Genom., 13.","DOI":"10.1186\/1471-2164-13-312"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Rana, S.B., Zadlock, F.J., Zhang, Z., Murphy, W.R., and Bentivegna, C.S. (2016). Comparison of de novo transcriptome assemblers and k-mer strategies using the killifish, Fundulus heteroclitus. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0153104"},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Nachtigall, P.G., Freitas-de-Sousa, L.A., Mason, A.J., Moura-da-Silva, A.M., Grazziotin, F.G., and Junqueira-de-Azevedo, I.L. (2022). Differences in PLA2 constitution distinguish the venom of two endemic Brazilian mountain Lanceheads, Bothrops cotiara and Bothrops fonsecai. Toxins, 14.","DOI":"10.3390\/toxins14040237"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1038\/nbt.1883","article-title":"Full-length transcriptome assembly from RNA-Seq data without a reference genome","volume":"29","author":"Grabherr","year":"2011","journal-title":"Nat. Biotechnol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1089\/cmb.2012.0021","article-title":"SPAdes: A new genome assembly algorithm and its applications to single-cell sequencing","volume":"19","author":"Bankevich","year":"2012","journal-title":"J. Comput. Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1093\/bioinformatics\/btu077","article-title":"SOAPdenovo-Trans: De novo transcriptome assembly with short RNA-Seq reads","volume":"30","author":"Xie","year":"2014","journal-title":"Bioinformatics"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1038\/nbt.3519","article-title":"Near-optimal probabilistic RNA-seq quantification","volume":"34","author":"Bray","year":"2016","journal-title":"Nat. Biotechnol."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Nachtigall, P.G., Rautsaw, R.M., Ellsworth, S.A., Mason, A.J., Rokyta, D.R., Parkinson, C.L., and Junqueira-de-Azevedo, I.L. (2021). ToxCodAn: A new toxin annotator and guide to venom gland transcriptomics. Brief. Bioinform., 22.","DOI":"10.1093\/bib\/bbab095"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1038\/s41587-021-01156-3","article-title":"SignalP 6.0 predicts all five types of signal peptides using protein language models","volume":"40","author":"Teufel","year":"2022","journal-title":"Nat. Biotechnol."},{"key":"ref_83","unstructured":"Posit Team (2024). RStudio: Integrated Development Environment for R. Posit Software, PBC. Available online: http:\/\/www.posit.co\/."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/5\/224\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T14:44:18Z","timestamp":1760107458000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/5\/224"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,5,11]]},"references-count":83,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2024,5]]}},"alternative-id":["toxins16050224"],"URL":"https:\/\/doi.org\/10.3390\/toxins16050224","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,5,11]]}}}