Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes

Pierre, Liam St.; Earl, Stephen; Filippovich, I V; Сорокина, Н. И.; Masci, Paul P.; Jersey, John de; Lavin, Martin F.

doi:10.1007/s00018-008-8573-5

Cited by 43 publications

(43 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Of note, hemotoxic effects are rarely observed in envenomation by Asiatic elapids due to the absence of procoagulant and hemorrhagic enzymes in their venoms [27]. On the other hand, the identification of Kunitz-type serine protease inhibitors (~7%, KSPI) in this study is in agreement with previous findings of KSPI from transcription activity in the venom-gland [28] and protein isolation from the venom [29] of Australian tiger snake. The role of KSPI in N. scutatus envenomation is unclear but potentially related to the facilitation of presynaptic neurotoxicity through ion channel inhibition and chaperoning the neurotoxic PLA 2 s [30,31].…”

Section: Proteome Of Notechis Scutatus Venomsupporting

confidence: 91%

Revisiting Notechis scutatus venom: on shotgun proteomics and neutralization by the “bivalent” Sea Snake Antivenom

Tan

2016

Journal of Proteomics

View full text Add to dashboard Cite

Section: Proteome Of Notechis Scutatus Venomsupporting

confidence: 91%

Revisiting Notechis scutatus venom: on shotgun proteomics and neutralization by the “bivalent” Sea Snake Antivenom

Tan

2016

Journal of Proteomics

View full text Add to dashboard Cite

“…Inter-specific variation is evident in the P3-P3' domain as well as the hairpin turn between beta sheets (residues 66-70) of all isoforms ( Figure 3). Textilinin-1,-2,-3 and -4 from a previous report [39] were identified in this study, as well as two more (textilinin -8 -9;…”

Section: Accepted M Manuscriptsupporting

confidence: 54%

“…textilis venom that show variation in the P3-P3' motif [39]. Textilinin-1 and -2 showed plasmin inhibition with both peptides containing an arginine residue at P1 while textilinin-3 (P1-asparagine) showed no inhibition [40].…”

Section: Accepted M Manuscriptmentioning

confidence: 99%

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

Reeks

Lavergne

Sunagar

et al. 2016

Journal of Proteomics

View full text Add to dashboard Cite

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.

show abstract

“…A great variety of BPTI transcripts were already described in elapid venom gland transcriptomes and some of them present an additional BPTI or wheyacidic-protein (WAP) domain St Pierre et al, 2008). WAP are peptides from the I17 serine proteases inhibitors family, found in large amounts in many mammals milk, and contain a domain found in many other proteins (Bingle et al, 2002;Hennighausen and Sippel, 1982).…”

Section: Serine Protease Inhibitors Peptides: Kunitz-like and Wapmentioning

confidence: 99%

Venomics of the Australian eastern brown snake ( Pseudonaja textilis ): Detection of new venom proteins and splicing variants

Viala

Hildebrand

Trusch

et al. 2015

Toxicon

View full text Add to dashboard Cite

The eastern brown snake is the predominant cause of snakebites in mainland Australia. Its venom induces defibrination coagulopathy, renal failure and microangiopathic hemolytic anemia. Cardiovascular collapse has been described as an early cause of death in patients, but, so far, the mechanisms involved have not been fully identified. In the present work, we analysed the venome of Pseudonaja textilis by combining high throughput proteomics and transcriptomics, aiming to further characterize the components of this venom. The combination of these techniques in the analysis and identification of toxins, venom proteins and putative toxins allowed the sequence description and the identification of the following: prothrombinase coagulation factors, neurotoxic textilotoxin phospholipase A2 (PLA2) subunits and "acidic PLA2", three-finger toxins (3FTx) and the Kunitz-type protease inhibitor textilinin, venom metalloproteinase, C-type lectins, cysteine rich secretory proteins, calreticulin, dipeptidase 2, as well as evidences of Heloderma lizard peptides. Deep data-mining analysis revealed the secretion of a new transcript variant of venom coagulation factor 5a and the existence of a splicing variant of PLA2 modifying the UTR and signal peptide from a same mature protein. The transcriptome revealed the diversity of transcripts and mutations, and also indicates that splicing variants can be an important source of toxin variation.

show abstract

Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes

Cited by 43 publications

References 38 publications

Revisiting Notechis scutatus venom: on shotgun proteomics and neutralization by the “bivalent” Sea Snake Antivenom

Revisiting Notechis scutatus venom: on shotgun proteomics and neutralization by the “bivalent” Sea Snake Antivenom

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

Venomics of the Australian eastern brown snake ( Pseudonaja textilis ): Detection of new venom proteins and splicing variants

Contact Info

Product

Resources

About