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Venom gland EST analysis of the saw-scaled viper, Echis ocellatus, reveals novel alpha(9)beta(1) integrin-binding motifs in venom metalloproteinases and a new group of putative toxins, renin-like aspartic proteases

Wagstaff, Simon ORCID: https://orcid.org/0000-0003-0577-5537 and Harrison, Robert (2006) 'Venom gland EST analysis of the saw-scaled viper, Echis ocellatus, reveals novel alpha(9)beta(1) integrin-binding motifs in venom metalloproteinases and a new group of putative toxins, renin-like aspartic proteases'. Gene, Vol 377, pp. 21-32.

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Abstract

Echis ocellatus is the most medically important snake in West Africa. However, the composition of its venom and the differential contribution of these venom components to the severe haemorrhagic and coagulopathic pathology of envenoming are poorly understood. To address this situation we assembled a toxin transcriptome based upon 1000 expressed sequence tags (EST) from a cDNA library constructed from pooled venom glands of 10 individual E. ocellatus. We used a variety of bioinformatic tools to construct a fully annotated venom-toxin transcriptome that was interrogated with a combination of BLAST annotation, gene ontology cataloguing and disintegrin-motif searching. The results of these analyses revealed an unusually abundant and diverse expression of snake venom metalloproteinases (SVMP) and a broad toxin-expression profile including several distinct isoforms of bradykinin-potentiatirig peptides, phospholipase A(2), C-type lectins, serine proteinases and L-amino oxidases. Most significantly, we identified for the first time a conserved alpha(9)beta(1) integrin-binding motif in several SVMPs, and a new group of putative venom toxins, renin-like aspartic proteases. (c) 2606 Elsevier B.V. All rights reserved.

Item Type: Article
Uncontrolled Keywords: viper venom metalloproteinase transcriptome cathepsin angiotensin-converting enzyme expressed sequence tags disintegrin-like domain c-type lectins snake-venom cell-adhesion gene-expression carpet viper integrin alpha(9)beta(1) phospholipases a(2)
Subjects: WD Disorders of Systemic, Metabolic or Environmental Origin, etc > Animal Poisons > WD 410 Reptiles
Faculty: Department: Groups (2002 - 2012) > Molecular & Biochemical Parasitology Group
Digital Object Identifer (DOI): https://doi.org/10.1016/j.gene.2006.03.008
Depositing User: Ms Julia Martin
Date Deposited: 02 Mar 2011 16:36
Last Modified: 17 Sep 2019 13:32
URI: https://archive.lstmed.ac.uk/id/eprint/1625

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