Cloning and characterisation of natriuretic peptides from the venom glands of Australian elapids

Pierre, Liam St.; Flight, Simone; Masci, Paul P.; Hanchard, Kim J.; Lewis, Richard J.; Alewood, Paul F.; Jersey, John de; Lavin, Martin F.

doi:10.1016/j.biochi.2006.06.014

Cited by 41 publications

(32 citation statements)

References 44 publications

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“…2N, spots 1 and 2). Natriuretic peptides were the only known protein family not found in the present study possibly due to their small molecular size (35-39 amino acids) (25).…”

Section: Discussionmentioning

confidence: 75%

“…Trypsin was added, and proteins were allowed to digest overnight at 37°C prior to extraction. Extracted peptides were dried; resuspended in 50% ACN, 0.1% TFA; mixed 1:1 with matrix (10 mg/ml ␣-cyano-4-hydroxycinamic acid in 60% acetonitrile, 25 January 11, 2006). In both cases, mass tolerance was set at 150 ppm.…”

Section: Methodsmentioning

confidence: 99%

“…Natriuretic peptides from Oxyuranus microlepidotus venom show potent arterial smooth muscle relaxant effects (24). Natriuretic peptides have been identified and characterized from several Australian elapid venoms and represent the smallest known proteins from these venoms at only 35-39 amino acids (25). The present study describes a thorough screening and identification of the venom proteins present in 18 Australian elapid snake species representing nine genera of the most venomous snakes on earth.…”

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confidence: 99%

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The Diversity of Bioactive Proteins in Australian Snake Venoms

Birrell

Earl

Wallis

et al. 2007

Molecular & Cellular Proteomics

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Australian elapid snakes are among the most venomous in the world. Their venoms contain multiple components that target blood hemostasis, neuromuscular signaling, and the cardiovascular system. We describe here a comprehensive approach to separation and identification of the venom proteins from 18 of these snake species, representing nine genera. The venom protein components were separated by two-dimensional PAGE and identified using mass spectrometry and de novo peptide sequencing. The venoms are complex mixtures showing up to 200 protein spots varying in size from <7 to over 150 kDa and in pI from 3 to >10. These include many proteins identified previously in Australian snake venoms, homologs identified in other snake species, and some novel proteins. In many cases multiple trains of spots were typically observed in the higher molecular mass range (>20 kDa) (indicative of posttranslational modification). Venom proteins and their posttranslational modifications were characterized using specific antibodies, phosphoprotein-and glycoprotein-specific stains, enzymatic digestion, lectin binding, and antivenom reactivity. In the lower molecular weight range, several proteins were identified, but the predominant species were phospholipase A 2 and ␣-neurotoxins, both represented by different sequence variants. The higher molecular weight range contained proteases, nucleotidases, oxidases, and homologs of mammalian coagulation factors. This information together with the identification of several novel proteins (metalloproteinases, vespryns, phospholipase A 2 inhibitors, protein-disulfide isomerase, 5-nucleotidases, cysteinerich secreted proteins, C-type lectins, and acetylcholinesterases) aids in understanding the lethal mechanisms of elapid snake venoms and represents a valuable resource for future development of novel human therapeutics.

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“…2N, spots 1 and 2). Natriuretic peptides were the only known protein family not found in the present study possibly due to their small molecular size (35-39 amino acids) (25).…”

Section: Discussionmentioning

confidence: 75%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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The Diversity of Bioactive Proteins in Australian Snake Venoms

Birrell

Earl

Wallis

et al. 2007

Molecular & Cellular Proteomics

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“…Both recombinant proteins were then further purified on an HPLC column before analysis on 15% SDS-PAGE stained with Coomassie and quantitated via a Lowry assay prior to functional analysis. Sizes of the recombinant proteins were also confirmed by MALDI-TOF analysis as previously described [16]. Electrophysiological recordings from bovine adrenal chromaffin cells.…”

Section: Methodsmentioning

confidence: 99%

Distinct activities of novel neurotoxins from Australian venomous snakes for nicotinic acetylcholine receptors

Pierre

Fischer

Adams

et al. 2007

Cell. Mol. Life Sci.

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Envenomation from Australian elapid snakes results in a myriad of neurological effects due to post-synaptic neurotoxins that bind and inhibit nicotinic acetylcholine receptors (nAChRs) of neurons and muscle fibres. However, despite the significant physiological effects of these toxins, they have remained largely undercharacterised at the molecular level. This study describes the identification and comparative analysis of multiple neurotoxin isoforms from ten Australian snakes, including functional characterisation of two of these isoforms, Os SNTX-1 from Oxyuranus scutellatus and the more potent Pt LNTX-1 from Pseudonaja textilis. Electrophysiological recordings from adrenal chromaffin cells demonstrate that both neurotoxins act as competitive antagonists of nAChRs in a concentration-dependent manner. Their effects upon spontaneous and nerve-evoked membrane responses at the amphibian neuromuscular junction provide further evidence that both toxins bind muscle nAChRs in an irreversible manner. This study represents one of the most comprehensive descriptions to date of the sequences and activity of individual Australian elapid neurotoxins.

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“…Among the 3 NPs (TNP-a, TNP-b, and TNP-c) isolated from the inland taipan, TNP-c was of similar potency to ANP and DNP, resulting in near complete relaxation in pre-contracted aortae [105]. Recently, St. Pierre et al [107,108] also reported comprehensive studies on the identification and comparative analysis of venom-gland-specific genes from Oxyuranus scutellatus (the costal taipan) and other snake species. Notably, from Pseudonaja textiles (the common brown snake), 2 isoforms (PtNP-a and PaNP-c) of an NP were found to inhibit angiotensin converting enzyme (ACE) in a dose-dependent manner [108].…”

Section: Dendroaspis Natriuretic Peptide and Other Snake Venomsmentioning

confidence: 95%

Natriuretic peptides and therapeutic applications

2007

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Since the discovery of atrial natriuretic factor by de Bold et al., there has been tremendous progress in our understanding of the physiologic, diagnostic and therapeutic roles of the natriuretic peptides (NPs) in health and disease. Natriuretic peptides are endogenous hormones that are released by the heart in response to myocardial stretch and overload. Three mammalian NPs have been identified and characterized, including atrial natriuretic peptide (ANP or atrial natriuretic factor), B-type natriuretic peptide (BNP), and C-type natriuretic peptide (CNP). In addition, Dendroaspis natriuretic peptide (DNP) has been isolated from the venom of Dendroaspis angusticeps (the green mamba snake), and urodilatin from human urine. These peptides are structurally similar and they consist of a 17-amino-acid core ring and a cysteine bridge. Both ANP and BNP bind to natriuretic peptide receptor A (NPR-A) that are expressed in the heart and other organs. Activation of NPR-A generates an increase in cyclic guanosine monophosphate, which mediates natriuresis, inhibition of renin and aldosterone, as well as vasorelaxant, anti-fibrotic, anti-hypertrophic, and lusitropic effects. The NP system thus serves as an important compensatory mechanism against neurohumoral activation in heart failure. This provides a strong rationale for the use of exogenous NPs in the management of acutely decompensated heart failure. In this article, the therapeutic applications of NPs in the acute heart failure syndromes are reviewed. Emerging therapeutic agents and areas for future research are discussed.

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Cloning and characterisation of natriuretic peptides from the venom glands of Australian elapids

Cited by 41 publications

References 44 publications

The Diversity of Bioactive Proteins in Australian Snake Venoms

The Diversity of Bioactive Proteins in Australian Snake Venoms

Distinct activities of novel neurotoxins from Australian venomous snakes for nicotinic acetylcholine receptors

Natriuretic peptides and therapeutic applications

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