Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8394927 | Toxicon | 2017 | 42 Pages |
Abstract
Snakebites are a serious health problem in tropical countries. In Brazil, the genus Bothrops (Viperidae family) causes most of the ophidic accidents, characterized by proteolysis and haemorrhage. Snake venoms are rich sources of toxins with great therapeutic and biotechnological potential and omics approaches is a valuable tool for identification of new bioactive components in the venom. In this study, we described the first transcriptome of the venom gland of Bothrops moojeni snake, using the next-generation sequencing with the Illumina platform. We identified: (i) 20 venom components classes, among which metalloproteases were the most expressed ones, followed by serine proteases and phospholipases; and (ii) the 33 full-length amino acid sequences of toxins that have never been reported before in B. moojeni venom, such as one cysteine-rich secretory protein (Moojin), two hyaluronidases (BmooHyal-1 and BmooHyal-2), and one three-finger toxin (Bmoo-3FTx). Altogether, the transcripts identified herein represent a starting point for the analysis of structure-function relationships of toxins, which shall help develop novel biological tools and therapeutic drugs.
Keywords
TPMSVSPSnake venom metalloproteasesTRUSVMPμgCystatinFPKMCTPSPHEPDEkDaNCBINaOHNGSGBPTSANaCll-amino acid oxidaseAminopeptidaseCRISPNext generation sequencingThree-finger toxinbase pairSraSequence Read Archivetranscripts per millionRINSnake venomSodium chlorideSerine proteaseRNA Integrity NumberGrowth factorPhosphodiesterasePhospholipasePhenylalanineLAAOC-type lectinTranscriptomicsNational Center for Biotechnology InformationProtease inhibitorTranscriptome shotgun assemblyBothrops moojeniHyalHyaluronidasesodium hydroxideCysteine-rich secretory proteinCathepsinquality controlkilodaltons
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Authors
Fernanda Gobbi Amorim, Romualdo Morandi-Filho, Patricia Tieme Fujimura, Carlos Ueira-Vieira, Suely Vilela Sampaio,