{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T11:16:49Z","timestamp":1788520609446,"version":"build-2803163510"},"reference-count":125,"publisher":"American Chemical Society (ACS)","issue":"5","license":[{"start":{"date-parts":[[2019,4,24]],"date-time":"2019-04-24T00:00:00Z","timestamp":1556064000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_ccby_termsofuse.html"}],"funder":[{"DOI":"10.13039\/501100004329","name":"Javna Agencija za Raziskovalno Dejavnost RS","doi-asserted-by":"publisher","award":["P1-0207"],"award-info":[{"award-number":["P1-0207"]}],"id":[{"id":"10.13039\/501100004329","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019,5,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The nose-horned viper, its nominotypical subspecies Vipera ammodytes ammodytes (Vaa), in particular, is, medically, one of the most relevant snakes in Europe. The local and systemic clinical manifestations of poisoning by the venom of this snake are the result of the pathophysiological effects inflicted by enzymatic and nonenzymatic venom components acting, most prominently, on the blood, cardiovascular, and nerve systems. This venom is a very complex mixture of pharmacologically active proteins and peptides. To help improve the current antivenom therapy toward higher specificity and efficiency and to assist drug discovery, we have constructed, by combining transcriptomic and proteomic analyses, the most comprehensive library yet of the Vaa venom proteins and peptides. Sequence analysis of the venom gland cDNA library has revealed the presence of messages encoding 12 types of polypeptide precursors. The most abundant are those for metalloproteinase inhibitors (MPis), bradykinin-potentiating peptides (BPPs), and natriuretic peptides (NPs) (all three on a single precursor), snake C-type lectin-like proteins (snaclecs), serine proteases (SVSPs), P-II and P-III metalloproteinases (SVMPs), secreted phospholipases A2 (sPLA2s), and disintegrins (Dis). These constitute &amp;gt;88% of the venom transcriptome. At the protein level, 57 venom proteins belonging to 16 different protein families have been identified and, with SVSPs, sPLA2s, snaclecs, and SVMPs, comprise \u223c80% of all venom proteins. Peptides detected in the venom include NPs, BPPs, and inhibitors of SVSPs and SVMPs. Of particular interest, a transcript coding for a protein similar to P-III SVMPs but lacking the MP domain was also found at the protein level in the venom. The existence of such proteins, also supported by finding similar venom gland transcripts in related snake species, has been demonstrated for the first time, justifying the proposal of a new P-IIIe subclass of ancestral SVMP precursor-derived proteins.<\/jats:p>","DOI":"10.1021\/acs.jproteome.9b00120","type":"journal-article","created":{"date-parts":[[2019,4,24]],"date-time":"2019-04-24T17:06:54Z","timestamp":1556125614000},"page":"2287-2309","source":"Crossref","is-referenced-by-count":51,"title":["Comprehensive\nStudy of the Proteome and Transcriptome\nof the Venom of the Most Venomous European Viper: Discovery of a New\nSubclass of Ancestral Snake Venom Metalloproteinase Precursor-Derived\nProteins"],"prefix":"10.1021","volume":"18","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9854-9955","authenticated-orcid":true,"given":"Adrijana","family":"Leonardi","sequence":"first","affiliation":[{"name":"Joz\u030cef Stefan Institute , , Jamova cesta 39 , ,","place":["Ljubljana, Slovenia, SI-1000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tamara","family":"Sajevic","sequence":"additional","affiliation":[{"name":"Joz\u030cef Stefan Institute , , Jamova cesta 39 , ,","place":["Ljubljana, Slovenia, SI-1000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7228-336X","authenticated-orcid":true,"given":"Joz\u030ce","family":"Pungerc\u030car","sequence":"additional","affiliation":[{"name":"Joz\u030cef Stefan Institute , , Jamova cesta 39 , ,","place":["Ljubljana, Slovenia, SI-1000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0203-0708","authenticated-orcid":true,"given":"Igor","family":"Kriz\u030caj","sequence":"additional","affiliation":[{"name":"Joz\u030cef Stefan Institute , , Jamova cesta 39 , ,","place":["Ljubljana, Slovenia, SI-1000"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2019,4,24]]},"reference":[{"key":"2026090406163881400_cit1","doi-asserted-by":"publisher","first-page":"1874","DOI":"10.2174\/0929867324666170605091546","article-title":"Snake venom:\nfrom deadly toxins to\nlife-saving therapeutics","volume":"24","author":"Waheed","year":"2017","journal-title":"Curr. 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Phylogenet. Evol."},{"key":"2026090406163881400_cit6","doi-asserted-by":"publisher","first-page":"1116","DOI":"10.1016\/j.ympev.2007.11.002","article-title":"Molecular phylogeography of the nose-horned\nviper (Vipera ammodytes, Linnaeus (1758)): Evidence\nfor high genetic diversity and multiple refugia in the Balkan peninsula","volume":"46","author":"Ursenbacher","year":"2008","journal-title":"Mol. Phylogenet. Evol."},{"key":"2026090406163881400_cit7","first-page":"191","article-title":"Venomous snakebites\nin southern Croatia","volume":"30","author":"Luks\u030cic\u0301","year":"2006","journal-title":"Coll. 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Biol."},{"key":"2026090406163881400_cit24","doi-asserted-by":"publisher","first-page":"609","DOI":"10.1016\/j.jprot.2008.10.003","article-title":"Combined\nsnake venomics and venom gland transcriptomic analysis of the ocellated\ncarpet viper, Echis ocellatus","volume":"71","author":"Wagstaff","year":"2009","journal-title":"J. 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Commun."},{"key":"2026090406163881400_cit28","doi-asserted-by":"publisher","first-page":"1158","DOI":"10.1016\/j.biochi.2013.01.003","article-title":"VaH3, one\nof the principal hemorrhagins in Vipera ammodytes ammodytes venom, is a homodimeric P-IIIc\nmetalloproteinase","volume":"95","author":"Sajevic","year":"2013","journal-title":"Biochimie"},{"key":"2026090406163881400_cit29","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1016\/j.biochi.2014.12.013","article-title":"Structural\nand biochemical characterisation\nof VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom","volume":"109","author":"Leonardi","year":"2015","journal-title":"Biochimie"},{"key":"2026090406163881400_cit30","doi-asserted-by":"publisher","first-page":"2637","DOI":"10.1093\/molbev\/msr091","article-title":"Domain loss\nfacilitates accelerated evolution and neofunctionalization of duplicate\nsnake venom metalloproteinase toxin genes","volume":"28","author":"Casewell","year":"2011","journal-title":"Mol.\nBiol. Evol."},{"key":"2026090406163881400_cit31","doi-asserted-by":"publisher","first-page":"292","DOI":"10.3390\/toxins8100292","article-title":"Novel catalytically-inactive PII metalloproteinases from a viperid\nsnake venom with substitutions in the canonical zinc-binding motif","volume":"8","author":"Camacho","year":"2016","journal-title":"Toxins"},{"key":"2026090406163881400_cit32","doi-asserted-by":"publisher","first-page":"e184","DOI":"10.1371\/journal.pmed.0030184","article-title":"Bioinformatics and multiepitope DNA\nimmunization to\ndesign rational snake antivenom","volume":"3","author":"Wagstaff","year":"2006","journal-title":"PLoS Med."},{"key":"2026090406163881400_cit33","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1016\/j.toxicon.2012.04.331","article-title":"First draft\nof the genomic organization\nof a PIII-SVMP gene","volume":"60","author":"Sanz","year":"2012","journal-title":"Toxicon"},{"key":"2026090406163881400_cit34","doi-asserted-by":"publisher","first-page":"1677","DOI":"10.1002\/1522-2683(200105)22:9&lt;1677::AID-ELPS1677&gt;3.0.CO;2-H","article-title":"An optimized\nprocedure for detection of proteins on carrier ampholyte isoelectric\nfocusing and immobilized pH gradient gels with imidazole and zinc\nsalts: Its application to the identification of isoelectric focusing\nseparated isoforms by in-gel proteolys","volume":"22","author":"Castellanos-Serra","year":"2001","journal-title":"Electrophoresis"},{"key":"2026090406163881400_cit35","doi-asserted-by":"publisher","first-page":"1736","DOI":"10.1016\/j.febslet.2009.03.029","article-title":"Venoms,\nvenomics, antivenomics","volume":"583","author":"Calvete","year":"2009","journal-title":"FEBS Lett."},{"key":"2026090406163881400_cit36","doi-asserted-by":"publisher","first-page":"909","DOI":"10.1002\/pmic.200700777","article-title":"Exploring snake\nvenom proteomes: Multifaceted analyses\nfor complex toxin mixtures","volume":"8","author":"Fox","year":"2008","journal-title":"Proteomics"},{"key":"2026090406163881400_cit37","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1042\/bj1530409","article-title":"Purification\nand properties of a kininogenin from the\nvenom of Vipera ammodytes ammodytes","volume":"153","author":"Bailey","year":"1976","journal-title":"Biochem. 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Biol. Chem."},{"key":"2026090406163881400_cit42","doi-asserted-by":"publisher","first-page":"1195","DOI":"10.1016\/S0969-2126(98)00119-1","article-title":"The crystal structure of the novel snake venom plasminogen activator\nTSV-PA: a prototype structure for snake venom serine proteinases","volume":"6","author":"Parry","year":"1998","journal-title":"Structure"},{"key":"2026090406163881400_cit43","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1016\/S0378-1119(00)00571-0","article-title":"Sequence diversity\nof Vipera lebetina snake venom gland serine proteinase homologs - result\nof alternative-splicing or genome alteration","volume":"263","author":"Siigur","year":"2001","journal-title":"Gene"},{"key":"2026090406163881400_cit44","doi-asserted-by":"publisher","first-page":"326","DOI":"10.1021\/pr060494k","article-title":"Snake venomics of Bitis gabonica gabonica. Protein family composition, subunit organization\nof venom toxins, and characterization of dimeric disintegrins bitisgabonin-1\nand bitisgabonin-2","volume":"6","author":"Calvete","year":"2007","journal-title":"J. Proteome Res."},{"key":"2026090406163881400_cit45","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1055\/s-0037-1613468","article-title":"Anticoagulant serine fibrinogenases\nfrom Vipera lebetina venom: Structure-function relationships","volume":"89","author":"Siigur","year":"2003","journal-title":"Thromb. 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