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Molecular cloning of Echis ocellatus disintegrins reveals non-venom-secreted proteins and a pathway for the evolution of ocellatusin

Juarez, P., Wagstaff, Simon ORCID:, Sanz, L., Harrison, Robert and Calvete, J. J. (2006) 'Molecular cloning of Echis ocellatus disintegrins reveals non-venom-secreted proteins and a pathway for the evolution of ocellatusin'. Journal of Molecular Evolution, Vol 63, Issue 2, pp. 183-193.

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We report the cloning and sequence analysis of Echis ocellatus cDNAs coding for dimeric disintegrin subunits and for the short disintegrin ocellatusin. All the dimeric disintegrin subunit messengers belong to the short-coding class, indicating that short messengers may be more widely distributed than previously thought. Mass spectrometric analysis of the HPLC-separated venom proteins was performed to characterize the dimeric disintegrins expressed in the venom proteome. In addition to previously reported EO4 and EO5 heterodimers, a novel dimeric disintegrin containing RGD- and KGD-bearing subunits was identified. However, a WGD-containing polypeptide encoded by clone Eo1-1 was not detected in the venom, suggesting the occurrence of larger genomic than proteomic diversity, which could represent part of a non-venom-secreted reservoir of disintegrin that may eventually acquire physiological relevance for the snake upon changes of ecological niches and prey habits. On the other hand, the realization of the existence of two distinct messengers coding for the short disintegrin ocellatusin reveals key events of the evolutionary emergence of the short disintegrin ocellatusin from a short-coding dimeric disintegrin precursor by two nucleotide mutations.

Item Type: Article
Uncontrolled Keywords: snake venom; echis ocellatus; cdna cloning; disintegrin evolution; ocellatusin precursor; disulfide-bond pattern; phylogenetic analysis; dimeric disintegrin; angstrom resolution; crystal-structure; toxin sequences; snake; viper origin antagonist
Subjects: QU Biochemistry > Genetics > QU 470 Genetic structures
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):
Depositing User: Ms Julia Martin
Date Deposited: 03 Mar 2011 13:58
Last Modified: 17 Sep 2019 13:32


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