Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka

Abstract

To examine the molecular diversity of the venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka, we isolated 38 venom proteins through a combination of anion exchange chromatography followed by reversed-phase high performance liquid chromatography. From the venom of D. r. russellii we isolated 15 proteins: 5 isozymes of phospholipase A 2 (PLA 2 ), 4 serine proteases, 2 C-type lectin-like proteins, 2 l-amino acid oxidases, 1 cysteine-rich secretory protein (CRISP), and 1 metalloproteinase. From the venom of N. naja we isolated 23 proteins: 10 isoforms of cytotoxins (CTX), 7 PLA 2 isozymes, 2 muscarinic toxinlike proteins, 2 CRISPs, 1 nerve growth factor, and 1 new thrombin-like serine protease. Most of these proteins contained new amino acid sequences for each species, indicating molecular diversity in venom proteins. The entire amino acid sequences of PLA 2 3 from D. r. russellii and CTX7 from N. naja were determined. Additionally, the polymorphic amino acid residues of PLA 2 3 were preferentially localized on the potential antigenic sites. While 2 types of PLA 2 (N and S types) were found in D. r. russellii (India) and D. r. siamensis (Java), all the PLA 2 s from D. r. siamensis (Burma) were N type, and those from D. r. russellii (Sri Lanka) were primarily S type.There are approximately 600 venomous species of snakes in the world. Although there are no accurate figures for the incidence of snakebites, at least 421,000 envenomings and 20,000 deaths are estimated to occur every year according to publications on snakebite and the World Health Organization (WHO) mortality database in 2008 (14). Snakebites caused by the families of Viperidae and Elapidae are particularly dangerous to humans. Not all the snakebites are fatal, yet they may result in the following conditions: permanent physical disability, including limb amputation; chronic ulceration; osteomyelitis with malignant transformation; chronic renal failure; chronic pituitary-adrenal insufficiency; Address correspondence to: Mieko Suzuki Division of Biomolecular Chemistry, Graduate School of Natural Sciences, Nagoya City University, Mizuho, Nagoya, 467-8501, Japan Tel: +81-52-872-5851, Fax: +81-52-872-5857 E-mail: m.suzuki@nsc.nagoya-cu.ac.jp To avoid confusion in terms of taxonomy, the following names were used in this paper:

Purification and partial characterization of an anticoagulant PLA2 from the venom of Indian Daboia russelii that induces inflammation through upregulation of proinflammatory mediators

“…The partial primary structure of Rv(i) PLA 2 was determined by peptide mass fingerprinting, which revealed that it belongs to group II PLA 2 family. It is a D49 PLA 2 that showed sequence similarity with basic PLA 2 (P86368) reported from Sri Lankan D. russelii whose functional property has not been revealed . Rv(i) PLA 2 , a calcium‐dependent enzyme, exhibited high catalytic activity when diheptanoyl‐thiophosphatidylcholine was used as a substrate.…”

The midgut transcriptome of Aedes aegypti fed with saline or protein meals containing chikungunya virus reveals genes potentially involved in viral midgut escape

“…UNC93A and SV seem to play a role in virus assembly and/or budding from the infected cell as revealed by transient gene silencing of SV2 or UNC93A in mosquitoes infected with SINV [37]. CRVP proteins are known to contain a trypsin inhibitor-like (TIL) domain, and therefore could be functioning as serine protease inhibitors [39]. One of the Ae.…”

Clinical and Pharmacological Investigation of Myotoxicity in Sri Lankan Russell’s Viper (Daboia russelii) Envenoming

“…The N-terminal sequence of the first 50 amino acids of the toxin ‘P1’ [31] and the N-terminal sequence of first 21 amino acids of the toxin PLA 2 4 [32] are a 100% match for the sequence of U1-viperitoxin-Dr1b. Following the suggested rational nomenclature for toxins [41], and given that the 94% sequence homology of the toxin with U1-viperitoxin-Dr1a[33], we have named the above toxin as U1-viperitoxin-Dr1b (Fig 6).…”

“…Myotoxic PLA 2 s cause muscle damage primarily by destruction of the sarcolemma [12,30]. Several PLA 2 toxins have been isolated from Sri Lankan Russell’s viper venom and biochemically characterised, [31,32] Some of these PLA 2 toxins contain a unique Serine residue at the N-terminus (S-type), while others have an Asparagine residue at the N-terminus (N-type) [32]. We have recently shown that the pre-synaptic neurotoxicity of the Sri Lankan Russell’s viper venom is primarily due to one of the S-type PLA 2 toxins, which we named U1-viperitoxin-Dr1a [33].…”