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The Venom of the Spine-Bellied Sea Snake (Hydrophis curtus): Proteome, Toxin Diversity and Intraspecific Variation.
Int J Mol Sci. 2017 Dec 12; 18(12)IJ

Abstract

The spine-bellied sea snake (Hydrophis curtus) is known to cause human deaths, yet its venom composition has not yet been proteomically characterised. An indepth proteomic analysis was performed on H. curtus venom from two different seasons, January and June, corresponding to adults and subadults, respectively. Venoms from adult and subadult H. curtus individuals were compared using reversedphase high-performance liquid chromatography (RP-HPLC), matrix-assisted laser desorption ionisation-time of flight (MALDI-TOF) mass spectrometry and liquid chromatography electrospray ionisation mass spectrometry (LC-ESI-MS) to detect intraspecific variation, and the molecular weight data obtained with ESIMS were used to assess toxin diversity. RPHPLC and LCESIMS/MS were used to characterise the venom proteome and estimate the relative abundances of protein families present. The most abundant protein family in January and June venoms is phospholipase A₂ (PLA₂: January 66.7%; June 54.5%), followed by threefinger toxins (3FTx: January 30.4%; June 40.4%) and a minor component of cysteine-rich secretory proteins (CRISP: January 2.5%; June 5%). Trace amounts of snake venom metalloproteinases (SVMP), C-type lectins and housekeeping and regulatory proteins were also found. Although the complexity of the venom is low by number of families present, each family contained a more diverse set of isoforms than previously reported, a finding that may have implications for the development of next-generation sea snake antivenoms. Intraspecific variability was shown to be minor with one obvious exception of a 14,157-Da protein that was present in some January (adult) venoms, but not at all in June (subadult) venoms. There is also a greater abundance of short-chain neurotoxins in June (subadult) venom compared with January (adult) venom. These differences potentially indicate the presence of seasonal, ontogenetic or sexual variation in H. curtus venom.

Authors+Show Affiliations

College of Public Health, Medical and Veterinary Sciences, James Cook University, McGregor Road, Smithfield, Cairns 4878, Australia. vanessa.neale@my.jcu.edu.au. Australian Institute of Tropical Health and Medicine (AITHM) and Centre for Biodiscovery and Molecular Development of Therapeutics (CBMDT), James Cook University, McGregor Road, Smithfield, Cairns 4878, Australia. vanessa.neale@my.jcu.edu.au.Australian Institute of Tropical Health and Medicine (AITHM) and Centre for Biodiscovery and Molecular Development of Therapeutics (CBMDT), James Cook University, McGregor Road, Smithfield, Cairns 4878, Australia. javier.sotillo@jcu.edu.au.Australian Institute of Tropical Health and Medicine (AITHM) and Centre for Biodiscovery and Molecular Development of Therapeutics (CBMDT), James Cook University, McGregor Road, Smithfield, Cairns 4878, Australia. jamie.seymour@jcu.edu.au.Australian Institute of Tropical Health and Medicine (AITHM) and Centre for Biodiscovery and Molecular Development of Therapeutics (CBMDT), James Cook University, McGregor Road, Smithfield, Cairns 4878, Australia. david.wilson4@jcu.edu.au.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

29231898

Citation

Neale, Vanessa, et al. "The Venom of the Spine-Bellied Sea Snake (Hydrophis Curtus): Proteome, Toxin Diversity and Intraspecific Variation." International Journal of Molecular Sciences, vol. 18, no. 12, 2017.
Neale V, Sotillo J, Seymour JE, et al. The Venom of the Spine-Bellied Sea Snake (Hydrophis curtus): Proteome, Toxin Diversity and Intraspecific Variation. Int J Mol Sci. 2017;18(12).
Neale, V., Sotillo, J., Seymour, J. E., & Wilson, D. (2017). The Venom of the Spine-Bellied Sea Snake (Hydrophis curtus): Proteome, Toxin Diversity and Intraspecific Variation. International Journal of Molecular Sciences, 18(12). https://doi.org/10.3390/ijms18122695
Neale V, et al. The Venom of the Spine-Bellied Sea Snake (Hydrophis Curtus): Proteome, Toxin Diversity and Intraspecific Variation. Int J Mol Sci. 2017 Dec 12;18(12) PubMed PMID: 29231898.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The Venom of the Spine-Bellied Sea Snake (Hydrophis curtus): Proteome, Toxin Diversity and Intraspecific Variation. AU - Neale,Vanessa, AU - Sotillo,Javier, AU - Seymour,Jamie E, AU - Wilson,David, Y1 - 2017/12/12/ PY - 2017/11/10/received PY - 2017/11/26/revised PY - 2017/11/27/accepted PY - 2017/12/13/entrez PY - 2017/12/13/pubmed PY - 2018/7/25/medline KW - Hydrophis curtus KW - intraspecific variation KW - sea snake venom KW - spine-bellied sea snake KW - venom proteome KW - venomics JF - International journal of molecular sciences JO - Int J Mol Sci VL - 18 IS - 12 N2 - The spine-bellied sea snake (Hydrophis curtus) is known to cause human deaths, yet its venom composition has not yet been proteomically characterised. An indepth proteomic analysis was performed on H. curtus venom from two different seasons, January and June, corresponding to adults and subadults, respectively. Venoms from adult and subadult H. curtus individuals were compared using reversedphase high-performance liquid chromatography (RP-HPLC), matrix-assisted laser desorption ionisation-time of flight (MALDI-TOF) mass spectrometry and liquid chromatography electrospray ionisation mass spectrometry (LC-ESI-MS) to detect intraspecific variation, and the molecular weight data obtained with ESIMS were used to assess toxin diversity. RPHPLC and LCESIMS/MS were used to characterise the venom proteome and estimate the relative abundances of protein families present. The most abundant protein family in January and June venoms is phospholipase A₂ (PLA₂: January 66.7%; June 54.5%), followed by threefinger toxins (3FTx: January 30.4%; June 40.4%) and a minor component of cysteine-rich secretory proteins (CRISP: January 2.5%; June 5%). Trace amounts of snake venom metalloproteinases (SVMP), C-type lectins and housekeeping and regulatory proteins were also found. Although the complexity of the venom is low by number of families present, each family contained a more diverse set of isoforms than previously reported, a finding that may have implications for the development of next-generation sea snake antivenoms. Intraspecific variability was shown to be minor with one obvious exception of a 14,157-Da protein that was present in some January (adult) venoms, but not at all in June (subadult) venoms. There is also a greater abundance of short-chain neurotoxins in June (subadult) venom compared with January (adult) venom. These differences potentially indicate the presence of seasonal, ontogenetic or sexual variation in H. curtus venom. SN - 1422-0067 UR - https://www.unboundmedicine.com/medline/citation/29231898/The_Venom_of_the_Spine_Bellied_Sea_Snake__Hydrophis_curtus_:_Proteome_Toxin_Diversity_and_Intraspecific_Variation_ L2 - https://www.mdpi.com/resolver?pii=ijms18122695 DB - PRIME DP - Unbound Medicine ER -