Platypus venom: source of novel compounds
Jennifer M. S. Koh A , Paramjit S. Bansal B , Allan M. Torres C and Philip W. Kuchel A DA School of Molecular and Microbial Biosciences, Building G08, University of Sydney, NSW 2006, Australia.
B Australian Nuclear Science and Technology Organisation, Menai, NSW 2234, Australia.
C Nanoscale Organisation and Dynamics Group, College of Health and Science, University of Western Sydney, Penrith South DC, NSW 1797, Australia.
D Corresponding author. Email: p.kuchel@mmb.usyd.edu.au
Australian Journal of Zoology 57(4) 203-210 https://doi.org/10.1071/ZO09040
Submitted: 7 April 2009 Accepted: 30 July 2009 Published: 26 October 2009
Abstract
An anatomical feature of the platypus (Ornithorhynchus anatinus) that is seen in only one other mammal, the echidna, is that the male has a crural glandular system that produces venom that is used for defence and territorial–breeding functions; whether the echidna is similarly venomous is not yet established. Platypus venom contains many novel proteins and peptides that are different from those in reptilian venom. It also causes pain and symptoms that are not experienced by any other kind of envenomation. Five types of proteins and peptides have been isolated and identified from platypus venom, namely: defensin-like peptides (DLPs); Ornithorhynchus venom C-type natriuretic peptides (OvCNPs); Ornithorhynchus nerve growth factor; hyaluronidase; and l-to-d-peptide isomerase. The structures of DLPs and OvCNPs have already been studied and they are very similar to β-defensin-12 and mammalian C-type natriuretic peptides, respectively. A special mammalian l-to-d-peptide isomerase that is responsible for interconverting the l- and d-peptide isomers is also found in platypus venom. Isomerase activity has recently been discovered in platypus tissues other than the venom gland. It is possible that similar kinds of enzymes might exist in other mammals and play important, as yet unknown, biological roles. Considering the fact that some animal venoms have already been widely used in pharmaceutical applications, research into platypus venom may lead to the discovery of new molecules and potent drugs that are useful biomedical tools.
Additional keywords: peptides, peptide isomerase, structure.
Acknowledgements
The work was funded by an ARC Discovery Project Grant to PWK and Associate Professor J. I. Vandenberg. Dr Dom Geraghty is thanked for discussions and the supply of venom and venom glands. JMSK is supported by an Australian Postgraduate Award.
Bansal, P. S. , Torres, A. M. , Crossett, B. , Wong, K. K. Y. , Koh, J. M. S. , Geraghty, D. P. , Vandenberg, J. I. , and Kuchel, P. W. (2008). Substrate specificity of platypus venom l-to-d-peptide isomerase. The Journal of Biological Chemistry 283, 8969–8975.
| Crossref | l-to-d-peptide isomerase.&journal=The Journal of Biological Chemistry&volume=283&pages=8969-8975&publication_year=2008&author=P%2E%20S%2E%20Bansal&hl=en&doi=10.1074/jbc.M709762200" target="_blank" rel="nofollow noopener noreferrer" class="reftools">GoogleScholarGoogle Scholar | CAS | PubMed |
Heck, S. D. , Siok, C. J. , Krapcho, K. J. , Kelbaugh, P. R. , and Thadeio, P. F. , et al. (1994). Functional consequences of posttranslational isomerization of ser(46) in a calcium-channel toxin. Science 266, 1065–1068.
| Crossref | GoogleScholarGoogle Scholar | CAS | PubMed |
Kostiza, T. , and Meier, J. (1996). Nerve growth factors from snake venoms: chemical properties, mode of action and biological significance. Toxicon 34, 787–806.
| Crossref | GoogleScholarGoogle Scholar | CAS | PubMed |
Torres, A. M. , and Kuchel, P. W. (2004). The beta-defensin-fold family of polypeptides. Toxicon 44, 581–588.
| Crossref | GoogleScholarGoogle Scholar | CAS | PubMed |
Torres, A. M. , Wang, X. H. , Fletcher, J. I. , Alewood, D. , and Alewood, P. F. , et al. (1999). Solution structure of a defensin-like peptide from platypus venom. The Biochemical Journal 341, 785–794.
| Crossref | GoogleScholarGoogle Scholar | CAS | PubMed |
Torres, A. M. , de Plater, G. M. , Doverskog, M. , Birinyi-Strachan, L. C. , Nicholson, G. M. , Gallagher, C. H. , and Kuchel, P. W. (2000). Defensin-like peptide-2 from platypus venom: member of a class of peptides with a distinct structural fold. The Biochemical Journal 348, 649–656.
| Crossref | GoogleScholarGoogle Scholar | CAS | PubMed |
Torres, A. M. , Alewood, D. , Alewood, P. F. , Gallagher, C. H. , and Kuchel, P. W. (2002). Conformations of platypus venom C-type natriuretic peptide in aqueous solution and sodium dodecyl sulfate micelles. Toxicon 40, 711–719.
| Crossref | GoogleScholarGoogle Scholar | CAS | PubMed |
Torres, A. M. , Tsampazi, C. , Geraghty, D. P. , Bansal, P. S. , Alewood, P. F. , and Kuchel, P. W. (2005). d-Amino acid residue in a defensin-like peptide from platypus venom: effect on structure and chromatographic properties. The Biochemical Journal 391, 215–220.
| Crossref | d-Amino acid residue in a defensin-like peptide from platypus venom: effect on structure and chromatographic properties.&journal=The Biochemical Journal&volume=391&pages=215-220&publication_year=2005&author=A%2E%20M%2E%20Torres&hl=en&doi=10.1042/BJ20050900" target="_blank" rel="nofollow noopener noreferrer" class="reftools">GoogleScholarGoogle Scholar | CAS | PubMed |
Torres, A. M. , Tsampazi, M. , Tsampazi, C. , Kennett, E. C. , Belov, K. , Geraghty, D. P. , Bansal, P. S. , Alewood, P. F. , and Kuchel, P. W. (2006). Mammalian l-to-d-amino-acid-residue isomerase from platypus venom. FEBS Letters 580, 1587–1591.
| Crossref | l-to-d-amino-acid-residue isomerase from platypus venom.&journal=FEBS Letters&volume=580&pages=1587-1591&publication_year=2006&author=A%2E%20M%2E%20Torres&hl=en&doi=10.1016/j.febslet.2006.01.089" target="_blank" rel="nofollow noopener noreferrer" class="reftools">GoogleScholarGoogle Scholar | CAS | PubMed |
Torres, A. M. , Tsampazi, M. , Kennett, E. C. , Belov, K. , Geraghty, D. P. , Bansal, P. S. , Alewood, P. F. , and Kuchel, P. W. (2007). Characterization and isolation of l-to-d-amino-acid-residue isomerase from platypus venom. Amino Acids 32, 63–68.
| Crossref | l-to-d-amino-acid-residue isomerase from platypus venom.&journal=Amino Acids&volume=32&pages=63-68&publication_year=2007&author=A%2E%20M%2E%20Torres&hl=en&doi=10.1007/s00726-006-0346-6" target="_blank" rel="nofollow noopener noreferrer" class="reftools">GoogleScholarGoogle Scholar | CAS | PubMed |
Whittington, C. M. , Papenfuss, A. T. , Kuchel, P. W. , and Belov, K. (2008). Expression patterns of platypus defensin and related venom genes across a range of tissue types reveal the possibility of broader functions for OvDLPs than previously suspected. Toxicon 52, 559–565.
| Crossref | GoogleScholarGoogle Scholar | CAS | PubMed |
Zimmermann, G. R. , Legault, P. , Selsted, M. E. , and Pardi, A. (1995). Solution structure of bovine neutrophil beta-defensin-12 – the peptide fold of the beta-defensins is identical to that of the classical defensins. Biochemistry 34, 13663–13671.
| Crossref | GoogleScholarGoogle Scholar | CAS | PubMed |
