Venomics of the Australian eastern brown snake (Pseudonaja textilis): Detection of new venom proteins and splicing variants
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Venomics of the Australian eastern brown snake (Pseudonaja textilis): Detection of new venom proteins and splicing variants. / Viala, Vincent Louis; Hildebrand, Diana; Trusch, Maria; Fucase, Tamara Mieco; Sciani, Juliana Mozer; Pimenta, Daniel Carvalho; Arni, Raghuvir K; Schlüter, Hartmut; Betzel, Christian; Mirtschin, Peter; Dunstan, Nathan; Spencer, Patrick Jack.
in: TOXICON, Jahrgang 107, Nr. Pt B, 01.12.2015, S. 252-65.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - Venomics of the Australian eastern brown snake (Pseudonaja textilis): Detection of new venom proteins and splicing variants
AU - Viala, Vincent Louis
AU - Hildebrand, Diana
AU - Trusch, Maria
AU - Fucase, Tamara Mieco
AU - Sciani, Juliana Mozer
AU - Pimenta, Daniel Carvalho
AU - Arni, Raghuvir K
AU - Schlüter, Hartmut
AU - Betzel, Christian
AU - Mirtschin, Peter
AU - Dunstan, Nathan
AU - Spencer, Patrick Jack
N1 - Copyright © 2015 Elsevier Ltd. All rights reserved.
PY - 2015/12/1
Y1 - 2015/12/1
N2 - The eastern brown snake is the predominant cause of snakebites in mainland Australia. Its venom induces defibrination coagulopathy, renal failure and microangiopathic hemolytic anemia. Cardiovascular collapse has been described as an early cause of death in patients, but, so far, the mechanisms involved have not been fully identified. In the present work, we analysed the venome of Pseudonaja textilis by combining high throughput proteomics and transcriptomics, aiming to further characterize the components of this venom. The combination of these techniques in the analysis and identification of toxins, venom proteins and putative toxins allowed the sequence description and the identification of the following: prothrombinase coagulation factors, neurotoxic textilotoxin phospholipase A2 (PLA2) subunits and "acidic PLA2", three-finger toxins (3FTx) and the Kunitz-type protease inhibitor textilinin, venom metalloproteinase, C-type lectins, cysteine rich secretory proteins, calreticulin, dipeptidase 2, as well as evidences of Heloderma lizard peptides. Deep data-mining analysis revealed the secretion of a new transcript variant of venom coagulation factor 5a and the existence of a splicing variant of PLA2 modifying the UTR and signal peptide from a same mature protein. The transcriptome revealed the diversity of transcripts and mutations, and also indicates that splicing variants can be an important source of toxin variation.
AB - The eastern brown snake is the predominant cause of snakebites in mainland Australia. Its venom induces defibrination coagulopathy, renal failure and microangiopathic hemolytic anemia. Cardiovascular collapse has been described as an early cause of death in patients, but, so far, the mechanisms involved have not been fully identified. In the present work, we analysed the venome of Pseudonaja textilis by combining high throughput proteomics and transcriptomics, aiming to further characterize the components of this venom. The combination of these techniques in the analysis and identification of toxins, venom proteins and putative toxins allowed the sequence description and the identification of the following: prothrombinase coagulation factors, neurotoxic textilotoxin phospholipase A2 (PLA2) subunits and "acidic PLA2", three-finger toxins (3FTx) and the Kunitz-type protease inhibitor textilinin, venom metalloproteinase, C-type lectins, cysteine rich secretory proteins, calreticulin, dipeptidase 2, as well as evidences of Heloderma lizard peptides. Deep data-mining analysis revealed the secretion of a new transcript variant of venom coagulation factor 5a and the existence of a splicing variant of PLA2 modifying the UTR and signal peptide from a same mature protein. The transcriptome revealed the diversity of transcripts and mutations, and also indicates that splicing variants can be an important source of toxin variation.
U2 - 10.1016/j.toxicon.2015.06.005
DO - 10.1016/j.toxicon.2015.06.005
M3 - SCORING: Journal article
C2 - 26079951
VL - 107
SP - 252
EP - 265
JO - TOXICON
JF - TOXICON
SN - 0041-0101
IS - Pt B
ER -