The Diversity of Bioactive Proteins in Australian Snake Venoms

Birrell, Geoff W.; Earl, Stephen; Wallis, Tristan P.; Masci, Paul P.; Jersey, John de; Gorman, Jeffrey J.; Lavin, Martin F.

doi:10.1074/mcp.m600419-mcp200

Cited by 86 publications

(71 citation statements)

References 65 publications

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“…Viperidae venoms are rich in enzymes that are typically observed in higher molecular mass regions (24). On the other hand, Elapidae venoms are known to possess a multitude of basic polypeptides, mainly neurotoxins and cardiotoxins (cytotoxin) that correspond to the lower range of molecular mass (13,25,26).…”

Section: Discussionmentioning

confidence: 99%

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

Vejayan¹,

Yee²,

Ponnudurai³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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Snake venoms comprise a highly complex mixture of proteins, which requires for their characterization the use of versatile two-dimensional electrophoresis techniques. In the present study, venoms obtained from eight snakes (Ophiophagus hannah, Naja kaouthia, Naja sumatrana, Bungarus fasciatus, Trimeresurus sumatranus, Tropidolaemus wagleri, Enhydrina schistosa and Calloselasma rhodostoma) commonly found in Malaysia were separated based on two independent properties, isoelectric point (pI) and molecular weight (MW). Many differences in snake venoms at the inter-family, inter-subfamily, inter-genus and inter-species levels were revealed. Notably, proteins from individuals of the Viperidae family -Trimeresurus sumatranus, Tropidolaemus wagleri and Calloselasma rhodostoma -were found to be numerous and scattered by the two-dimensional gel electrophoresis (2DE) specifically in regions between 37 and 100 kDa compared to the Elapidae venom proteins. The latter were clustered at the basic and lower molecular mass region (less than 20 kDa). Trains of spots were commonly observed, indicating that these proteins may be derived from post-translational modifications. Ophiophagus hannah (Elapidae) revealed a great amount of protein spots in the higher molecular mass range when compared to Enhydrina schistosa, Naja kaouthia, Naja sumatrana and Bungarus fasciatus. Overall 2DE showed large differences in the venom profile of each species, which might be employed as an ancillary tool to the identification of venomous snake species.

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Section: Discussionmentioning

confidence: 99%

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

Vejayan¹,

Yee²,

Ponnudurai³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

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“…Furthermore, investigation of Australian elapid venom has mainly focused on the isolation and characterization of the most toxic or abundant protein components that are readily observed by 2D gel chromatography [1].…”

Section: Accepted M Manuscriptmentioning

confidence: 99%

“…Elapid venoms contain numerous protein and peptide families that act as enzymes or ligands of membrane bound receptors with agonist or inhibitory mechanisms of action [1]. A number of families, such as the phospholipase A 2 (PLA 2 ) enzymes, and three finger toxins (3FTxs) exhibit conserved structural frameworks that present a broad range of pharmacological effects [2].…”

Section: Introductionmentioning

confidence: 99%

Deep venomics of the Pseudonaja genus reveals inter- and intra-specific variation

Reeks

Lavergne

Sunagar

et al. 2016

Journal of Proteomics

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Australian elapid venom remains an under-investigated resource of novel bioactive peptides. In this study, the venom gland transcriptomes and proteomes of the Australian western brown snakes, Pseudonaja aspidorhyncha and Pseudonaja nuchalis, were compared to Pseudonaja textilis. A deep venomics strategy incorporating high throughput 454 pyrosequencing gave a total of 200,911 raw reads for the three venoms. Subsequent annotation identified 5716 transcripts from 20 different toxin families with inter-specific variation between species observed in eight of the less abundant families. Integration of each venom proteome with the corresponding annotated reads identified 65 isoforms from six toxin families; high sequence coverage highlighted subtle differences between sequences and intra and inter-specific variation between species. High quality MS/MS data identified unusual glycoforms with natriuretic peptides from P. aspidorhyncha and P. nuchalis containing O-linked trisaccharides with high homology to the glycosylated region of TNPc. Molecular evolutionary assessments indicated the accelerated evolution of all toxin families with the exception of both natriuretic peptides and P. aspidorhyncha PLA2s that were found to be evolutionarily constrained under purifying selection pressures. This study has revealed a wide range of novel peptide sequences from six bioactive peptide families and highlights the subtle differences between toxins in these closely related species. Biological SignificanceMining Australia's vastly untapped source of toxins from its venomous creatures has been significantly advanced by employing deep venomics methodology.Technological advances in transcriptome analysis using next generation sequencing platforms and proteome analysis by highly sensitive tandem mass spectrometry allowed a more comprehensive interrogation of three underinvestigated brown snake (Pseudonaja) venoms uncovering many novel peptide sequences that are unique to these closely related species. This generic strategy will provide invaluable information when applied to other venomous snakes for a deeper understanding of venom composition, envenomation, venom evolution, as well as identifying research tools and drug leads.

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“…SVMPs are more abundantly found in viper snake venom; however, they are also from few elapid families (Birrell et al, 2007;Fry et al, 2003). They are synthesized as zymogens in the venom gland and contain a propeptide which is cleaved off during maturation.…”

Section: Introductionmentioning

confidence: 99%

Identification of accelerated evolution in the metalloproteinase domain of snake venom metalloproteinase sequences (SVMPs) through comparative analysis

Islam¹,

Roly²,

Ruhullah³

et al. 2016

Afr. J. Biotechnol.

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Computational protein sequence analysis is one of the most important tools used for understanding the evolution of closely related proteins sequences including snake venom metalloproteinase sequences (SVMPs) which give valuable information regarding genetic variations. The fundamental objective of the present study is to screen the evolution distributed in metalloproteinase domain regions of protein sequences among different SVMPs in snake species which are involved in a range of pathological disorders such as arthritis, atherosclerosis, liver fibrosis, cardiovascular, cancer, liver and neurodegenerative disorders. In fact, SVMPS are responsible for hemorrhage and may also interfere with the hemostatic system. A comparative characterization of the metalloproteinase sequences has been carried out to analyze their multiple sequence alignment, phylogenic tree, homology, physicochemical, secondary structural and functional properties. DNAMAN software was used for multiple sequence alignment, phylogenic tree and homology and Expasy's Prot-param server was used for amino acid composition, physico-chemical and functional characterization of these SVMPs sequences. Studies of secondary structure of these SVMPs were carried out by computational program. Based on the observed patterns of occurrence of atypical features, we hypothesize that amino acids of metalloproteinase domain region (66.63% identity) of protein sequences are highly changeable; whereas, signal peptide region (93.98% identity) is the lowest changeable protein sequence and the remaining other three domains such as propeptide region (87.36% identity), desintegrin domain region (78.63% identity) and cysteine-rich domain region (75.70% identity) show moderate changeable protein sequence. SVMPs might be an accelerated evolution, which is a key player in causing diseases. From the data, it can be suggested that over -changed metalloproteinase domain regions in snake venom metalloproteinase might be responsible for the generation of functional variation of proteins expressed, which in turn may lead to different disorders in humans after snake bite. The results of this study would be an effective tool for the study of mutation, drugs resistance mechanisms and development of new drugs for different diseases.

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The Diversity of Bioactive Proteins in Australian Snake Venoms

Cited by 86 publications

References 65 publications

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

Protein profile analysis of Malaysian snake venoms by two-dimensional gel electrophoresis

Deep venomics of the Pseudonaja genus reveals inter- and intra-specific variation

Identification of accelerated evolution in the metalloproteinase domain of snake venom metalloproteinase sequences (SVMPs) through comparative analysis

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