Proteomic characterization and comparison of Malaysian Bungarus candidus and Bungarus fasciatus venoms

• Venom proteomes of Malaysian Bungarus candidus and Bungarus fasciatus were compared
• We found that there are at least 18 different venom protein families in the venoms
• Higher number of proteins were identified in B. candidus compared to B. fasciatus venom
• Several protein families that have not previously been reported in the venoms were detected

Kraits (Bungarus spp.) are highly venomous elapids that are only found in Asia. In the current study, 103 and 86 different proteins were identified from Bungarus candidus and Bungarus fasciatus venoms, respectively. These proteins were classified into 18 different venom protein families. Both venoms were found to contain a high percentage of three finger toxins, phospholipase A2 enzymes and Kunitz-type inhibitors. Smaller number of high molecular weight enzymes such as L-amino acid oxidase, hyaluronidases, and acetylcholinesterase were also detected in the venoms. We also detected some unique proteins that were not known to be present in these venoms. The presence of a natriuretic peptide, vespryn, and serine protease families was detected in B. candidus venom. We also detected the presence of subunit A and B of β-bungarotoxin and α-bungarotoxin which had not been previously found in B. fasciatus venom. Understanding the proteome composition of Malaysian krait species will provide useful information on unique toxins and proteins which are present in the venoms. This knowledge will assist in the management of krait envenoming. In addition, these proteins may have potential use as research tools or as drug-design templates.Biological significanceThis study has revealed the proteome composition of Malaysian B. candidus and B. fasciatus venoms, two medically important snake species in Asia. Information on the venom proteome of these species will provide useful information for krait bite management and aid in antivenom selection. Venom proteome profiles of these venoms showed that there are significant differences in the venom protein family compositions. Detection of proteins and peptides that have not been documented in these species such as natriuretic peptides, vespryn and serine proteases provides new knowledge on the composition of these venoms. The roles of these new proteins and peptides in krait envenoming are still unknown. Discovery of these proteins and peptides may also be useful for future research tool and therapeutic development.

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