Identification of cDNAs encoding viper venom hyaluronidases: Cross-generic sequence conservation of full-length and unusually short variant transcripts

Harrison, Robert, Ibison, Frances, Wilbraham, Davina and Wagstaff, Simon ORCID: https://orcid.org/0000-0003-0577-5537 (2007) 'Identification of cDNAs encoding viper venom hyaluronidases: Cross-generic sequence conservation of full-length and unusually short variant transcripts'. Gene, Vol 392, Issue 1-2, pp. 22-33.

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Abstract

The immobilisation of prey by snakes is most efficiently achieved by the rapid dissemination of venom from its site of injection into the blood stream. Hyaluronidase is a common component of snake venoms and has been termed the "venom spreading factor". In the absence of nucleotide or protein sequence data to confirm the functional identity of this venom component, we interrogated a venom gland EST database for the saw-scaled viper, Echis ocellatus (Nigeria), using the gene ontology (GO) term "carbohydrate metabolism". A single hyalurononglucosaminadase-activity matching sequence (EOC00242) was found and used to design PCR primers to acquire the full-length cDNA sequence. Although very different from the bee venom and mammalian hyaluronidase sequences, the E. ocellatus sequence retained all the catalytic, positional and structural residues that characterise this class of carbohydrate metabolising hydrolases. An extraordinarily high level of sequence identity (>95%) was observed in analogous venom gland cDNA sequences isolated (by PCR) from another saw-scaled viper species, E. pyramidum leakeyi (Kenya), and from the sahara homed viper, Cerastes cerastes cerastes (Egypt) and the puff adder, Bitis arietans (Nigeria). Smaller amplicons, lacking hyaluronidase catalytic residues because of 768 bp or 855 bp central deletions, appear to encode either truncated peptides without hyaluronidase activity, or are non-translated transcripts because they lack consensus translation initiating motifs.

Item Type:	Article
Uncontrolled Keywords:	viper venom hyaluronidase echis bitis cerastes naja-naja venom polyacrylamide-gel-electrophoresis local tissue-damage snake-venom extracellular-matrix molecular evolution phospholipases a(2) agkistrodon-acutus spreading factor echis
Subjects:	QU Biochemistry > Genetics > QU 450 General Works 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.2006.10.026
Depositing User:	Mary Creegan
Date Deposited:	02 Nov 2010 09:32
Last Modified:	17 Jul 2020 10:57
URI:	https://archive.lstmed.ac.uk/id/eprint/1203

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