Show simple item record

dc.creatorMackessy, Stephen P.
dc.creatorBryan, Wendy
dc.creatorSmith, Cara F.
dc.creatorLopez, Keira
dc.creatorFernández Ulate, Julián
dc.creatorBonilla Murillo, Fabián
dc.creatorCamacho Umaña, Erika
dc.creatorSasa Marín, Mahmood
dc.creatorLomonte, Bruno
dc.description.abstractRear-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.es_ES
dc.sourceJournal of Proteomics (2020) 220, 103778es_ES
dc.subjectsnake venomes_ES
dc.titleVenomics of the Central American Lyre snake Trimorphodon quadruplex (Colubridae: Smith, 1941) from Costa Ricaes_ES
dc.typeartículo científicoes_ES
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES

Files in this item


There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record