Venomics of the Central American Lyre snake Trimorphodon quadruplex (Colubridae: Smith, 1941) from Costa Rica
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| Autores: | , , , , , , , , |
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| Formato: | artículo original |
| Fecha de Publicación: | 2020 |
| Descripción: | Rear-fanged colubrid snakes include hundreds of species globally that possess a Duvernoy's venom gland and often one-several enlarged rear maxillary teeth. We investigated the venom proteome of the Central American Lyre Snake (Trimorphodon quadruplex), a moderate-sized rear-fanged colubrid snake and the southernmost Trimorphodon, using a bottom-up proteomic approach coupled with enzyme and inhibitor assays, cytotoxicity assays and lethal toxicity assays. Several enzymes uncommonly observed in colubrid venoms were purified and characterized further. Trimorphodon quadruplex has a rather low complexity venome, typical of many rear-fanged snakes, but its venom contains L-amino acid oxidase, phospholipase A2, and a dimeric 3FTx, and 3FTxs dominate the proteome. Its PLA2 is catalytically quite active, but it lacks myotoxicity or acute toxicity; LAAO exhibits conserved structure and appears to be highly labile. Several P-III metalloproteinases are present and hydrolyze azocasein and the α-subunit of fibrinogen but lack hemorrhagic activity. Trimorphodon quadruplex produces venom and retains constriction, utilizing both chemically-mediated and mechanical feeding modes. |
| País: | Kérwá |
| Institución: | Universidad de Costa Rica |
| Repositorio: | Kérwá |
| Lenguaje: | Inglés |
| OAI Identifier: | oai:kerwa.ucr.ac.cr:10669/82966 |
| Acceso en línea: | https://www.sciencedirect.com/science/article/abs/pii/S1874391920301469?via%3Dihub https://hdl.handle.net/10669/82966 |
| Palabra clave: | proteomics snake venom Colubridae |