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Biochem J. Jun 15, 2000; 348(Pt 3): 649–656.
PMCID: PMC1221109

Defensin-like peptide-2 from platypus venom: member of a class of peptides with a distinct structural fold.

Abstract

The venom of the male Australian duck-billed platypus contains a family of four polypeptides of appox. 5 kDa, which are referred to as defensin-like peptides (DLPs). They are unique in that their amino acid sequences have no significant similarities to those of any known peptides; however, the tertiary structure of one of them, DLP-1, has recently been shown to be similar to beta-defensin-12 and to the sodium neurotoxin peptide ShI (Stichodactyla helianthus neurotoxin I). Although DLPs are the major peptides in the platypus venom, little is known about their biological roles. In this study, we determined the three-dimensional structure of DLP-2 by NMR spectroscopy, with the aim of gaining insights into the natural function of the DLPs in platypus venom. The DLP-2 structure was found to incorporate a short helix that spans residues 9-12, and an antiparallel beta-sheet defined by residues 15-18 and 37-40. The overall fold and cysteine-pairing pattern of DLP-2 were found to be similar to those of DLP-1, and hence beta-defensin-12; however, the sequence similarities between the three molecules are relatively small. The distinct structural fold of the DLP-1, DLP-2, and beta-defensin-12 is based upon several key residues that include six cysteines. DLP-3 and DLP-4 are also likely to be folded similarly since they have high sequence similarity with DLP-2. The DLPs, and beta-defensin-12 may thus be grouped together into a class of polypeptide molecules which have a common or very similar global fold. The fact that the DLPs did not display antimicrobial, myotoxic, or cell-growth-promoting activities implies that the nature of the side chains in this group of peptides is likely to play an important role in defining the biological function(s).

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Selected References

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  • Fenner PJ, Williamson JA, Myers D. Platypus envenomation--a painful learning experience. Med J Aust. 1992 Dec 7;157(11-12):829–832. [PubMed]
  • Torres AM, Wang X, Fletcher JI, Alewood D, Alewood PF, Smith R, Simpson RJ, Nicholson GM, Sutherland SK, Gallagher CH, et al. Solution structure of a defensin-like peptide from platypus venom. Biochem J. 1999 Aug 1;341(Pt 3):785–794. [PMC free article] [PubMed]
  • de Plater G, Martin RL, Milburn PJ. A pharmacological and biochemical investigation of the venom from the platypus (Ornithorhynchus anatinus). Toxicon. 1995 Feb;33(2):157–169. [PubMed]
  • de Plater GM, Martin RL, Milburn PJ. The natriuretic peptide (ovCNP-39) from platypus (Ornithorhynchus anatinus) venom relaxes the isolated rat uterus and promotes oedema and mast cell histamine release. Toxicon. 1998 Jun;36(6):847–857. [PubMed]
  • Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. J Biol Chem. 1993 Mar 25;268(9):6641–6648. [PubMed]
  • Zimmermann GR, Legault P, Selsted ME, Pardi A. Solution structure of bovine neutrophil beta-defensin-12: the peptide fold of the beta-defensins is identical to that of the classical defensins. Biochemistry. 1995 Oct 17;34(41):13663–13671. [PubMed]
  • Marion D, Wüthrich K. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. Biochem Biophys Res Commun. 1983 Jun 29;113(3):967–974. [PubMed]
  • Rance M, Sørensen OW, Bodenhausen G, Wagner G, Ernst RR, Wüthrich K. Improved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filtering. Biochem Biophys Res Commun. 1983 Dec 16;117(2):479–485. [PubMed]
  • Piotto M, Saudek V, Sklenár V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR. 1992 Nov;2(6):661–665. [PubMed]
  • Güntert P, Mumenthaler C, Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997 Oct 17;273(1):283–298. [PubMed]
  • Mumenthaler C, Braun W. Automated assignment of simulated and experimental NOESY spectra of proteins by feedback filtering and self-correcting distance geometry. J Mol Biol. 1995 Dec 1;254(3):465–480. [PubMed]
  • Mumenthaler C, Güntert P, Braun W, Wüthrich K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination. J Biomol NMR. 1997 Dec;10(4):351–362. [PubMed]
  • Hutchinson EG, Thornton JM. PROMOTIF--a program to identify and analyze structural motifs in proteins. Protein Sci. 1996 Feb;5(2):212–220. [PMC free article] [PubMed]
  • Ludvigsen S, Poulsen FM. Positive theta-angles in proteins by nuclear magnetic resonance spectroscopy. J Biomol NMR. 1992 May;2(3):227–233. [PubMed]
  • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol. 1993 Sep 5;233(1):123–138. [PubMed]
  • Fogh RH, Kem WR, Norton RS. Solution structure of neurotoxin I from the sea anemone Stichodactyla helianthus. A nuclear magnetic resonance, distance geometry, and restrained molecular dynamics study. J Biol Chem. 1990 Aug 5;265(22):13016–13028. [PubMed]
  • Wilcox GR, Fogh RH, Norton RS. Refined structure in solution of the sea anemone neurotoxin ShI. J Biol Chem. 1993 Nov 25;268(33):24707–24719. [PubMed]
  • Gould AR, Mabbutt BC, Llewellyn LE, Goss NH, Norton RS. Linear and cyclic peptide analogues of the polypeptide cardiac stimulant, anthopleurin-A. 1H-NMR and biological activity studies. Eur J Biochem. 1992 Jun 15;206(3):641–651. [PubMed]
  • Fox JW, Elzinga M, Tu AT. Amino acid sequence and disulfide bond assignment of myotoxin a isolated from the venom of Prairie rattlesnake (Crotalus viridis viridis). Biochemistry. 1979 Feb 20;18(4):678–684. [PubMed]
  • Mebs D, Ownby CL. Myotoxic components of snake venoms: their biochemical and biological activities. Pharmacol Ther. 1990;48(2):223–236. [PubMed]
  • Schweitz H, Vigne P, Moinier D, Frelin C, Lazdunski M. A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps). J Biol Chem. 1992 Jul 15;267(20):13928–13932. [PubMed]
  • Barfaraz A, Harvey AL. The use of the chick biventer cervicis preparation to assess the protective activity of six international reference antivenoms on the neuromuscular effects of snake venoms in vitro. Toxicon. 1994 Mar;32(3):267–272. [PubMed]
  • Dyck PJ, Peroutka S, Rask C, Burton E, Baker MK, Lehman KA, Gillen DA, Hokanson JL, O'Brien PC. Intradermal recombinant human nerve growth factor induces pressure allodynia and lowered heat-pain threshold in humans. Neurology. 1997 Feb;48(2):501–505. [PubMed]
  • Barton GJ. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 1993 Jan;6(1):37–40. [PubMed]
  • Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph. 1996 Feb;14(1):51–32. [PubMed]

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