Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes

St Pierre, L., Earl, E., Filippovich, I., Sorokina, N., Masci, P., De Jersey, J. and Lavin, M. F. (2008) Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes. Cellular And Molecular Life Sciences, 65 24: 4039-4054. doi:10.1007/s00018-008-8573-5

Author St Pierre, L.
Earl, E.
Filippovich, I.
Sorokina, N.
Masci, P.
De Jersey, J.
Lavin, M. F.
Title Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes
Journal name Cellular And Molecular Life Sciences   Check publisher's open access policy
ISSN 1420-682X
Publication date 2008-01-01
Sub-type Article (original research)
DOI 10.1007/s00018-008-8573-5
Open Access Status Not yet assessed
Volume 65
Issue 24
Start page 4039
End page 4054
Total pages 16
Editor Jolles, P
Place of publication Basel, Switzerland
Publisher Birkhaeuser Verlag AG
Language eng
Subject C1
970106 Expanding Knowledge in the Biological Sciences
110106 Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
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.
Keyword Elapid
Kunitz-like inhibitors
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2009 Higher Education Research Data Collection
UQ Centre for Clinical Research Publications
School of Medicine Publications
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Citation counts: TR Web of Science Citation Count  Cited 30 times in Thomson Reuters Web of Science Article | Citations
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Created: Tue, 31 Mar 2009, 01:09:04 EST by Carmen Buttery on behalf of UQ Centre for Clinical Research