{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T22:12:51Z","timestamp":1793052771394,"version":"4.5.0"},"reference-count":97,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2018,9,5]],"date-time":"2018-09-05T00:00:00Z","timestamp":1536105600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Ciencia y Tecnolog\u00eda","doi-asserted-by":"publisher","award":["237864"],"award-info":[{"award-number":["237864"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006087","name":"Direcci\u00f3n General de Asuntos del Personal Acad\u00e9mico, Universidad Nacional Aut\u00f3noma de M\u00e9xico","doi-asserted-by":"publisher","award":["IN203416"],"award-info":[{"award-number":["IN203416"]}],"id":[{"id":"10.13039\/501100006087","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>To understand the diversity of scorpion venom, RNA from venomous glands from a sawfinger scorpion, Serradigitus gertschi, of the family Vaejovidae, was extracted and used for transcriptomic analysis. A total of 84,835 transcripts were assembled after Illumina sequencing. From those, 119 transcripts were annotated and found to putatively code for peptides or proteins that share sequence similarities with the previously reported venom components of other species. In accordance with sequence similarity, the transcripts were classified as potentially coding for 37 ion channel toxins; 17 host defense peptides; 28 enzymes, including phospholipases, hyaluronidases, metalloproteases, and serine proteases; nine protease inhibitor-like peptides; 10 peptides of the cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 protein superfamily; seven La1-like peptides; and 11 sequences classified as \u201cother venom components\u201d. A mass fingerprint performed by mass spectrometry identified 204 components with molecular masses varying from 444.26 Da to 12,432.80 Da, plus several higher molecular weight proteins whose precise masses were not determined. The LC-MS\/MS analysis of a tryptic digestion of the soluble venom resulted in the de novo determination of 16,840 peptide sequences, 24 of which matched sequences predicted from the translated transcriptome. The database presented here increases our general knowledge of the biodiversity of venom components from neglected non-buthid scorpions.<\/jats:p>","DOI":"10.3390\/toxins10090359","type":"journal-article","created":{"date-parts":[[2018,9,6]],"date-time":"2018-09-06T02:55:07Z","timestamp":1536202507000},"page":"359","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4882-7491","authenticated-orcid":false,"given":"Maria Teresa","family":"Romero-Guti\u00e9rrez","sequence":"first","affiliation":[{"name":"Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnolog\u00eda, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6062-282X","authenticated-orcid":false,"given":"Carlos Eduardo","family":"Santib\u00e1\u00f1ez-L\u00f3pez","sequence":"additional","affiliation":[{"name":"Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnolog\u00eda, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico"},{"name":"Department of Integrative Biology, University of Wisconsin\u2013Madison, Madison, WI 53706, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9508-9332","authenticated-orcid":false,"given":"Juana Mar\u00eda","family":"Jim\u00e9nez-Vargas","sequence":"additional","affiliation":[{"name":"Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnolog\u00eda, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cesar Vicente Ferreira","family":"Batista","sequence":"additional","affiliation":[{"name":"Laboratorio Universitario de Prote\u00f3mica, Instituto de Biotecnolog\u00eda, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8713-0224","authenticated-orcid":false,"given":"Ernesto","family":"Ortiz","sequence":"additional","affiliation":[{"name":"Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnolog\u00eda, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6357-2661","authenticated-orcid":false,"given":"Lourival Domingos","family":"Possani","sequence":"additional","affiliation":[{"name":"Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnolog\u00eda, Universidad Nacional Aut\u00f3noma de M\u00e9xico, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,9,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1206\/830.1","article-title":"Redefinition and generic revision of the north american Vaejovid scorpion subfamily Syntropinae Kraepelin 1905, with descriptions of six new genera","volume":"382","author":"Prendini","year":"2013","journal-title":"Bull. Am. Museum Nat. Hist."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Santib\u00e1\u00f1ez-L\u00f3pez, C.E., Francke, O.F., Ureta, C., and Possani, L. (2015). Scorpions from Mexico: From species diversity to venom complexity. Toxins, 8.","DOI":"10.3390\/toxins8010002"},{"key":"ref_3","first-page":"113","article-title":"Substratum specialization and speciation in southern African scorpions: The Effect Hypothesis revisited","volume":"2001","author":"Prendini","year":"2001","journal-title":"Scorpions"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.toxicon.2010.10.008","article-title":"Vejovine, a new antibiotic from the scorpion venom of Vaejovis mexicanus","volume":"57","author":"Balderas","year":"2011","journal-title":"Toxicon"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"4049","DOI":"10.1021\/bi300060n","article-title":"Structure, function, and chemical synthesis of Vaejovis mexicanus peptide 24: A novel potent blocker of Kv1.3 potassium channels of human T lymphocytes","volume":"51","author":"Gurrola","year":"2012","journal-title":"Biochemistry"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1124\/mol.112.078006","article-title":"Vm24, a natural immunosuppressive peptide, potently and selectively blocks Kv1.3 potassium channels of human T cells","volume":"82","author":"Varga","year":"2012","journal-title":"Mol. Pharmacol."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Quintero-Hern\u00e1ndez, V., Ram\u00edrez-Carreto, S., Romero-Guti\u00e9rrez, M.T., Valdez-Vel\u00e1zquez, L.L., Becerril, B., Possani, L.D., and Ortiz, E. (2015). Transcriptome analysis of scorpion species belonging to the Vaejovis genus. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0117188"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Romero-Gutierrez, T., Peguero-Sanchez, E., Cevallos, M.A., Batista, C.V.F., Ortiz, E., and Possani, L.D. (2017). A deeper examination of Thorellius atrox scorpion venom components with omic techonologies. Toxins, 9.","DOI":"10.3390\/toxins9120399"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.toxicon.2018.06.085","article-title":"The diversity of venom components of the scorpion species Paravaejovis schwenkmeyeri (Scorpiones: Vaejovidae) revealed by transcriptome and proteome analyses","volume":"151","author":"Meneses","year":"2018","journal-title":"Toxicon"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1111\/cla.12091","article-title":"Phylogeny of the north american vaejovid scorpion subfamily Syntropinae Kraepelin, 1905, based on morphology, mitochondrial and nuclear DNA","volume":"31","author":"Prendini","year":"2015","journal-title":"Cladistics"},{"key":"ref_11","first-page":"1","article-title":"Scorpions of Baja California, Mexico, and adjacent islands","volume":"135","author":"Williams","year":"1980","journal-title":"Occas. Pap. Calif. Acad. Sci."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1146\/annurev.en.32.010187.001423","article-title":"Scorpion bionomics","volume":"32","author":"Williams","year":"1987","journal-title":"Ann. Rev. Entomol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.jprot.2015.07.030","article-title":"Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis","volume":"128","author":"Zhang","year":"2015","journal-title":"J. Proteom."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.toxicon.2017.01.014","article-title":"Venom-gland transcriptomics and venom proteomics of the black-back scorpion (Hadrurus spadix) reveal detectability challenges and an unexplored realm of animal toxin diversity","volume":"128","author":"Rokyta","year":"2017","journal-title":"Toxicon"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.toxicon.2017.12.042","article-title":"Venom-gland transcriptomics and venom proteomics of the Hentz striped scorpion (Centruroides hentzi; Buthidae) reveal high toxin diversity in a harmless member of a lethal family","volume":"142","author":"Ward","year":"2018","journal-title":"Toxicon"},{"key":"ref_16","unstructured":"Baradaran, M., Jalali, A., Soorki, M., Jokar, M., and Galehdari, H. (2018). First transcriptome analysis of Iranian scorpion, Mesobuthus eupeus venom gland. Iran. J. Pharm. Res., in press."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.jprot.2016.08.004","article-title":"Transcriptomic analysis of the venom glands from the scorpion Hadogenes troglodytes revealed unique and extremely high diversity of the venom peptides","volume":"150","author":"Zhong","year":"2017","journal-title":"J. Proteom."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.toxicon.2017.05.002","article-title":"Venom gland transcriptomic and venom proteomic analyses of the scorpion Megacormus gertschi D\u00edaz-Najera, 1966 (Scorpiones: Euscorpiidae: Megacorminae)","volume":"133","author":"Zamudio","year":"2017","journal-title":"Toxicon"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Santib\u00e1\u00f1ez-L\u00f3pez, C.E., Cid-Uribe, J.I., Batista, C.V.F., Ortiz, E., and Possani, L.D. (2016). Venom gland transcriptomic and proteomic analyses of the enigmatic scorpion Superstitionia donensis (Scorpiones: Superstitioniidae), with insights on the evolution of its venom components. Toxins, 8.","DOI":"10.3390\/toxins8120367"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.toxicon.2017.12.051","article-title":"De novo transcriptomic analysis of the venomous glands from the scorpion Heterometrus spinifer revealed unique and extremely high diversity of the venom peptides","volume":"143","author":"Deng","year":"2018","journal-title":"Toxicon"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.toxicon.2006.09.016","article-title":"Novel paradigms on scorpion toxins that affects the activating mechanism of sodium channels","volume":"49","author":"Possani","year":"2007","journal-title":"Toxicon"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.toxicon.2012.03.022","article-title":"Mapping of scorpion toxin receptor sites at voltage-gated sodium channels","volume":"60","author":"Gurevitz","year":"2012","journal-title":"Toxicon"},{"key":"ref_23","first-page":"81","article-title":"The systematics of the scorpion subfamily Uroctoninae (Scorpiones: Chactidae)","volume":"10","author":"Soleglad","year":"2004","journal-title":"Rev. Ib\u00e9r. Aracnol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"4753","DOI":"10.1111\/j.1432-1033.2004.04439.x","article-title":"Phaiodotoxin, a novel structural class of insect-toxin isolated from the venom of the Mexican scorpion Anuroctonus phaiodactylus","volume":"271","author":"Batista","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1242\/jeb.205.6.869","article-title":"Cn11, the first example of a scorpion toxin that is a true blocker of Na+ currents in crayfish neurons","volume":"205","author":"Garcia","year":"2002","journal-title":"J. Exp. Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.abb.2017.12.012","article-title":"Intraspecific variation of Centruroides sculpturatus scorpion venom from two regions of Arizona","volume":"638","author":"Rowe","year":"2018","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"baw056","DOI":"10.1093\/database\/baw056","article-title":"Kalium: A database of potassium channel toxins from scorpion venom","volume":"2016","author":"Kuzmenkov","year":"2016","journal-title":"Database"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.neuropharm.2017.09.025","article-title":"Arthropod toxins acting on neuronal potassium channels","volume":"127","author":"Possani","year":"2017","journal-title":"Neuropharmacology"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"10478","DOI":"10.1073\/pnas.1103501108","article-title":"Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif","volume":"108","author":"Smith","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.toxicon.2017.01.012","article-title":"Corrigendum to \u201cThe first report on transcriptome analysis of the venom gland of Iranian scorpion, Hemiscorpius lepturus\u201d [Toxicon 125 (2017) 123\u2013130]","volume":"128","author":"Torabi","year":"2017","journal-title":"Toxicon"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.toxicon.2012.11.017","article-title":"Characterization of the venom from the Australian scorpion Urodacus yaschenkoi: Molecular mass analysis of components, cDNA sequences and peptides with antimicrobial activity","volume":"63","author":"Batista","year":"2013","journal-title":"Toxicon"},{"key":"ref_32","unstructured":"Possani-Postay, L.D., Gurrola-Briones, G., Salas-Castillo, S.P., Batista, C.V.F., Varga, Z.S., Panyi, G., and G\u00e1sp\u00e1r, R. (2007). Vm23 and Vm24, Two Scorpion Peptides that Block Human T-Lymphocyte Potassium Channels (Sub-Type Kv1.3) with High Selectivity and Decrease the In Vivo DTH-Response in Rats. (EP2158213A1), European Patent."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.peptides.2006.06.012","article-title":"Wide phylogenetic distribution of Scorpine and long-chain beta-KTx-like peptides in scorpion venoms: Identification of \u201corphan\u201d components","volume":"28","author":"Schwartz","year":"2007","journal-title":"Peptides"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.toxicon.2016.07.010","article-title":"First venom gland transcriptomic analysis of Iranian yellow scorpion Odonthubuthus doriae","volume":"120","author":"Soorki","year":"2016","journal-title":"Toxicon"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Schwartz, E.F., Diego-Garcia, E., de la Vega, R.C.R., 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_36","doi-asserted-by":"crossref","unstructured":"Chen, Z., Luo, F., Feng, J., Yang, W., Zeng, D., Zhao, R., Cao, Z., Liu, M., Li, W., and Jiang, L. (2013). Genomic and structural characterization of Kunitz-Type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0060201"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Garc\u00eda-Fern\u00e1ndez, R., Peigneur, S., Pons, T., Alvarez, C., Gonz\u00e1lez, L., Ch\u00e1vez, M.A., and Tytgat, J. (2016). The kunitz-type protein ShPI-1 inhibits serine proteases and voltage-gated potassium channels. Toxins, 8.","DOI":"10.3390\/toxins8040110"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1002\/prot.10588","article-title":"Evolutionary trace analysis of scorpion toxins specific for K+-channels","volume":"54","author":"Zhu","year":"2004","journal-title":"Proteins Struct. Funct. Genet."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1016\/j.peptides.2011.05.017","article-title":"The new kappa-KTx 2.5 from the scorpion Opisthacanthus cayaporum","volume":"32","author":"Camargos","year":"2011","journal-title":"Peptides"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/j.bcp.2012.01.021","article-title":"Purification, molecular cloning and functional characterization of HelaTx1 (Heterometrus laoticus): The first member of a new k-KTX subfamily","volume":"83","author":"Vandendriessche","year":"2012","journal-title":"Biochem. Pharmacol."},{"key":"ref_41","first-page":"12185","article-title":"Scorpion toxins targeted against the sarcoplasmic reticulum Ca(2+)-release channel of skeletal and cardiac muscle","volume":"89","author":"Valdivia","year":"1992","journal-title":"Physiology"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1085\/jgp.201511499","article-title":"Structure\u2013function relationships of peptides forming the calcin family of ryanodine receptor ligands","volume":"147","author":"Xiao","year":"2016","journal-title":"J. Gen. Physiol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"8906","DOI":"10.1073\/pnas.1214062110","article-title":"Multiple actions of phi-LITX-Lw1a on ryanodine receptors reveal a functional link between scorpion DDH and ICK toxins","volume":"110","author":"Smith","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1096\/fj.02-1044fje","article-title":"Evolutionary origin of inhibitor cystine knot peptides","volume":"17","author":"Zhu","year":"2003","journal-title":"FASEB J."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1042\/BJ20061404","article-title":"Hemicalcin, a new toxin from the Iranian scorpion Hemiscorpius lepturus which is active on ryanodine-sensitive Ca2+ channels","volume":"404","author":"Shahbazzadeh","year":"2007","journal-title":"Biochem. J."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/0014-2999(94)90303-4","article-title":"Effect of omega-agatoxin-IVA on autonomic neurotransmission","volume":"261","author":"Lundy","year":"1994","journal-title":"Eur. J. Pharmacol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"ii17","DOI":"10.1136\/ard.62.suppl_2.ii17","article-title":"Roles of antimicrobial peptides such as defensins in innate and adaptive immunity","volume":"62","author":"Oppenheim","year":"2003","journal-title":"Ann. Rheum. Dis."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/s00441-010-1022-4","article-title":"Defensins in innate immunity","volume":"343","author":"Hazlett","year":"2011","journal-title":"Cell Tissue Res."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1128\/CMR.00056-05","article-title":"Peptide antimicrobial agents","volume":"19","author":"Jenssen","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1007\/s00018-004-4096-x","article-title":"Antimicrobial peptide induction in the haemolymph of the Mexican scorpion Centruroides limpidus limpidus in response to septic injury","volume":"61","author":"Scaloni","year":"2004","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"e3142","DOI":"10.7717\/peerj.3142","article-title":"Comparative venom gland transcriptomics of Naja kaouthia (monocled cobra) from Malaysia and Thailand: Elucidating geographical venom variation and insights into sequence novelty","volume":"5","author":"Tan","year":"2017","journal-title":"PeerJ"},{"key":"ref_52","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_53","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_54","doi-asserted-by":"crossref","unstructured":"Inagaki, H. (2017). Snake venom proteases inhibitors: Enhanced identification, expanding biological function, and promising future. Snake Venoms, Toxinology, Springer.","DOI":"10.1007\/978-94-007-6410-1_16"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.peptides.2013.10.021","article-title":"Scorpion venom peptides with no disulfide bridges: A review","volume":"51","author":"Almaaytah","year":"2014","journal-title":"Peptides"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.toxicon.2014.11.233","article-title":"Scorpion venom components as potential candidates for drug development","volume":"93","author":"Ortiz","year":"2015","journal-title":"Toxicon"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.peptides.2015.08.014","article-title":"Peptides from the scorpion Vaejovis punctatus with broad antimicrobial activity","volume":"73","author":"Corzo","year":"2015","journal-title":"Peptides"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/j.peptides.2012.02.002","article-title":"Gene cloning and functional characterization of four novel antimicrobial-like peptides from scorpions of the family Vaejovidae","volume":"34","author":"Corzo","year":"2012","journal-title":"Peptides"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/j.toxicon.2004.03.022","article-title":"Current views on scorpion toxins specific for K+-channels","volume":"43","author":"Possani","year":"2004","journal-title":"Toxicon"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1736","DOI":"10.1016\/j.ijbiomac.2018.07.016","article-title":"Mass spectrometry-assisted venom profiling of Hypnale hypnale found in the Western Ghats of India incorporating de novo sequencing approaches","volume":"118","author":"Vanuopadath","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Walter, A., Bechsgaard, J., Scavenius, C., Dyrlund, T.S., Sanggaard, K.W., Enghild, J.J., and Bilde, T. (2017). Characterisation of protein families in spider digestive fluids and their role in extra-oral digestion. BMC Genom., 18.","DOI":"10.1186\/s12864-017-3987-9"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/S0003-2697(02)00404-9","article-title":"Unmasking venom gland transcriptomes in reptile venoms","volume":"311","author":"Chen","year":"2002","journal-title":"Anal. Biochem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.toxicon.2014.12.013","article-title":"The transcriptome recipe for the venom cocktail of Tityus bahiensis scorpion","volume":"95","author":"Candido","year":"2015","journal-title":"Toxicon"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1016\/j.toxicon.2005.02.029","article-title":"Hemorrhage induced by snake venom metalloproteinases: Biochemical and biophysical mechanisms involved in microvessel damage","volume":"45","author":"Gutierrez","year":"2005","journal-title":"Toxicon"},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Hass, E., and Stanley, D. (2007). Phospholipases. xPharm: The Comprehensive Pharmacology Reference, Elsevier.","DOI":"10.1016\/B978-008055232-3.63043-0"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"958797","DOI":"10.1155\/2013\/958797","article-title":"Scorpion peptides: Potential use for new drug development","volume":"2013","author":"Hmed","year":"2013","journal-title":"J. Toxicol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.toxicon.2011.05.016","article-title":"Heminecrolysin, the first hemolytic dermonecrotic toxin purified from scorpion venom","volume":"58","author":"Borchani","year":"2011","journal-title":"Toxicon"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Vines, C.M., and Bill, C.A. (2015). Phospholipases. eLS, Wiley Online Library.","DOI":"10.1002\/9780470015902.a0001394.pub3"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1186\/s40409-015-0042-7","article-title":"Arthropod venom Hyaluronidases: Biochemical properties and potential applications in medicine and biotechnology","volume":"21","author":"Bordon","year":"2015","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1159\/000322847","article-title":"Hyaluronidase and hyaluronan in insect venom allergy","volume":"156","author":"King","year":"2011","journal-title":"Int. Arch. Allergy Immunol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/1678-9199-20-2","article-title":"Purification and characterization of a hyaluronidase from venom of the spider Vitalius dubius (Araneae, Theraphosidae)","volume":"20","author":"Sutti","year":"2014","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Luna-Ram\u00edrez, K., Quintero-Hern\u00e1ndez, V., Ju\u00e1rez-Gonz\u00e1lez, V.R., and Possani, L.D. (2015). Whole transcriptome of the venom gland from Urodacus yaschenkoi scorpion. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0127883"},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Amorim, F.G., Costa, T.R., Baiwir, D., De Pauw, E., Quinton, L., and Sampaio, S.V. (2018). Proteopeptidomic, functional and immunoreactivity characterization of Bothrops moojeni snake venom: Influence of snake gender on venom composition. Toxins, 10.","DOI":"10.3390\/toxins10050177"},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Kazuma, K., Masuko, K., Konno, K., and Inagaki, H. (2017). Combined venom gland transcriptomic and venom peptidomic analysis of the predatory ant Odontomachus monticola. Toxins, 9.","DOI":"10.3390\/toxins9100323"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.cbpc.2018.01.004","article-title":"Toxic activity and protein identification from the parotoid gland secretion of the common toad Bufo bufo","volume":"205","author":"Kowalski","year":"2018","journal-title":"Comp. Biochem. Physiol. Part C Toxicol. Pharmacol."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Silva-Lib\u00e9rio, M., Bastos, I., J\u00fanior, O., Fontes, W., Santana, J., and Castro, M. (2014). The crude skin secretion of the pepper frog Leptodactylus labyrinthicus is rich in metallo and serine peptidases. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0096893"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1007\/978-1-4939-6673-8_18","article-title":"Killing bacteria with cytotoxic effector proteins of human killer immune cells: Granzymes, granulysin, and perforin","volume":"1535","author":"Fellay","year":"2017","journal-title":"Methods Mol. Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/S2221-1691(13)60175-6","article-title":"Evaluation of cytotoxic and anti-tumor activity of partially purified serine protease isolate from the Indian earthworm Pheretima posthuma","volume":"3","author":"Vema","year":"2013","journal-title":"Asian Pac. J. Trop. Biomed."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1016\/j.intimp.2013.02.023","article-title":"Effects of two serine proteases from Bothrops pirajai snake venom on the complement system and the inflammatory response","volume":"15","author":"Menaldo","year":"2013","journal-title":"Int. Immunopharmacol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/S0041-0101(98)00205-0","article-title":"Natural protease inhibitors to hemorrhagins in snake venoms and their potential use in medicine","volume":"37","year":"1999","journal-title":"Toxicon"},{"key":"ref_81","first-page":"607","article-title":"Protease inhibitor in scorpion (Mesobuthus eupeus) venom prolongs the biological activities of the crude venom","volume":"14","author":"Ma","year":"2016","journal-title":"Chin. J. Nat. Med."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.euprot.2017.02.001","article-title":"Novel Kazal-tyoe proteinase inhibitors from the skin secretion of the Splendid leaf frog, Cruziohyla calcarifer","volume":"15","author":"Li","year":"2017","journal-title":"EuPA Open Proteom."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.cbpb.2009.02.010","article-title":"A novel serine protease inhibitor from the venom of Vespa bicolor Fabricius","volume":"153","author":"Yang","year":"2009","journal-title":"Comp. Biochem. Physiol. Part B Biochem. Mol. Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.toxicon.2015.09.004","article-title":"A new Kunitz-type plasmin inhibitor from scorpion venom","volume":"106","author":"Ding","year":"2015","journal-title":"Toxicon"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1002\/psc.2778","article-title":"Chemical synthesis of La1 isolated from the venom of the scorpion Liocheles australasiae and determination of its disulfide bonding pattern","volume":"21","author":"Nagao","year":"2015","journal-title":"J. Pept. Sci."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/j.toxicon.2007.04.012","article-title":"Characterization of peptide components in the venom of the scorpion Liocheles australasiae (Hemiscorpiidae)","volume":"50","author":"Miyashita","year":"2007","journal-title":"Toxicon"},{"key":"ref_87","first-page":"116","article-title":"Spermaurin, an La1-like peptide from the venom of the scorpion Scorpio maurus plamatus, improves sperm motility and fertilization in different mammalian species","volume":"23","author":"Martinez","year":"2017","journal-title":"Mol. Hum. Reprod."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1210\/er.2008-0032","article-title":"The CAP superfamily: Cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins\u2014Roles in reproduction, cancer, and immune defense","volume":"29","author":"Gibbs","year":"2008","journal-title":"Endocr. Rev."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/nature04328","article-title":"Early evolution of the venom system in lizards and snakes","volume":"439","author":"Fry","year":"2006","journal-title":"Nature"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"3313","DOI":"10.1002\/dvdy.21738","article-title":"Cysteine-rich secretory proteins are not exclusively expressed in the male reproductive tract","volume":"237","author":"Reddy","year":"2008","journal-title":"Dev. Dyn."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Almeida, D., Scortecci, K., Kobashi, L., Agnez-Lima, L., Medeiros, S., Silva-Junior, A., Junqueira-de-Azevedo, I., and Fernandes-Pedrosa, M. (2012). Profiling the resting venom gland of the scorpion Tityus stigmurus through a transcriptomic survey. BMC Genom., 13.","DOI":"10.1186\/1471-2164-13-362"},{"key":"ref_92","first-page":"761","article-title":"The insulin-like growth factor-binding protein (IGFBP) superfamily","volume":"20","author":"Hwa","year":"1999","journal-title":"Endocr. Rev."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1016\/j.celrep.2016.12.063","article-title":"A tissue-mapped axolotl de novo transcriptome enables identification of limb regeneration factors","volume":"18","author":"Bryant","year":"2017","journal-title":"Cell Rep."},{"key":"ref_94","first-page":"74","article-title":"The turbidimetric assay of hyaluronidase","volume":"34","author":"Tolksdorf","year":"1949","journal-title":"J. Lab. Clin. Med."},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Horta, C.C.R., de Magalh\u00e3es, B.F., Oliveira-Mendes, B.B.R., Carmo, A.O.D., Duarte, C.G., Felicori, L.F., Machado-de-\u00c1vila, R.A., Ch\u00e1vez-Ol\u00f3rtegui, C., and Kalapothakis, E. (2014). Molecular, immunological, and biological characterization of Tityus serrulatus venom hyaluronidase: New insights into its role in envenomation. PLoS Negl. Trop. Dis., 8.","DOI":"10.1371\/journal.pntd.0002693"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/0003-2697(72)90495-2","article-title":"A sensitive and specific plate test for the quantitation of phospholipases","volume":"50","author":"Habermann","year":"1972","journal-title":"Anal. Biochem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1590\/S1678-91992004000300005","article-title":"Purification and partial characterization of phospholipases A2 from Bothrops asper (barba amarilla) snake venom from Chiriguan\u00e1 (Cesar, Colombia)","volume":"10","author":"Quevedo","year":"2004","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/10\/9\/359\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T15:18:56Z","timestamp":1760195936000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/10\/9\/359"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,9,5]]},"references-count":97,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2018,9]]}},"alternative-id":["toxins10090359"],"URL":"https:\/\/doi.org\/10.3390\/toxins10090359","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,9,5]]}}}