Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes |
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| Authors: | L St Pierre S T Earl I Filippovich N Sorokina P P Masci J De Jersey M F Lavin |
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| Institution: | (1) The Queensland Cancer Fund Research Unit, The Queensland Institute of Medical Research, P.O. Box Royal Brisbane Hospital, Herston, Brisbane, 4029, Australia;(2) Center for Clinical Research, The University of Queensland, Brisbane, Australia;(3) School of Medicine, Southern Clinical Division, The University of Queensland, Brisbane, Australia |
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| Abstract: | The venoms of Australian snakes contain a myriad of pharmacologically active toxin components. This study describes the identification
and comparative analysis of two distinct toxin families, the kunitztype serine protease inhibitors and waprins, and demonstrates
a previously unknown evolutionary link between the two. Multiple cDNA and full-length gene isoforms were cloned and shown
to be composed of three exons separated by two introns. A high degree of identity was observed solely within the first exon
which coded for the propeptide sequence and its cleavage site, and indicates that each toxin family has arisen from a gene
duplication event followed by diversification only within the portion of the gene coding for the functional toxin. It is proposed
that while the mechanism of toxin secretion is highly conserved, diversification of mature toxin sequences allows for the
existence of multiple protein isoforms in the venom to adapt to variations within the prey environment. |
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