Multifunctional warheads: diversification of the toxin arsenal of centipedes via novel multidomain transcripts

Undheim, Eivind A. B., Sunagar, Kartik, Hamilton, Brett R., Jones, Alun, Venter, Deon J., Fry, Bryan G. and King, Glenn F. (2014) Multifunctional warheads: diversification of the toxin arsenal of centipedes via novel multidomain transcripts. Journal of Proteomics, 102 1-10. doi:10.1016/j.jprot.2014.02.024


Author Undheim, Eivind A. B.
Sunagar, Kartik
Hamilton, Brett R.
Jones, Alun
Venter, Deon J.
Fry, Bryan G.
King, Glenn F.
Title Multifunctional warheads: diversification of the toxin arsenal of centipedes via novel multidomain transcripts
Journal name Journal of Proteomics   Check publisher's open access policy
ISSN 1874-3919
1876-7737
Publication date 2014-05-06
Sub-type Article (original research)
DOI 10.1016/j.jprot.2014.02.024
Open Access Status Not Open Access
Volume 102
Start page 1
End page 10
Total pages 10
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Language eng
Abstract Arthropod toxins are almost invariably encoded by transcripts encoding prepropeptides that are posttranslationally processed to yield a single mature toxin. In striking contrast to this paradigm, we used a complementary transcriptomic, proteomic and MALDI-imaging approach to identify four classes of multidomain centipede-toxin transcripts that each encodes multiple mature toxins. These multifunctional warheads comprise either: (1) repeats of linear peptides; (2) linear peptides preceding cysteine-rich peptides; (3) cysteine-rich peptides preceding linear peptides; or (4) repeats of linear peptides preceding cysteine-rich peptides. MALDI imaging of centipede venom glands revealed that these peptides are posttranslationally liberated from the original gene product in the venom gland and not by proteases following venom secretion. These multidomain transcripts exhibit a remarkable conservation of coding sequences, in striking contrast to monodomain toxin transcripts from related centipede species, and we demonstrate that they represent a rare class of predatory toxins that have evolved under strong negative selection. We hypothesize that the peptide toxins liberated from multidomain precursors might have synergistic modes of action, thereby allowing negative selection to dominate as the toxins encoded by the same transcript become increasingly interdependent.
Keyword Centipede venom
Multidomain transcript
Evolution
Posttranslational modification
MALDI imaging
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

 
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Created: Tue, 18 Mar 2014, 23:34:32 EST by Susan Allen on behalf of Institute for Molecular Bioscience