A proteomic analysis of Pakistan Daboia russelii russelii venom and assessment of potency of Indian polyvalent and monovalent antivenom

Mukherjee, Ashis K.; Kalita, Bhargab; Mackessy, Stephen P.

doi:10.1016/j.jprot.2016.06.001

Cited by 76 publications

(165 citation statements)

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“…Similar proteome analysis of D. russelii from Pakistan and Sri Lanka identified PLA 2 enzymes as the most abundant toxins. Analysis of Pakistan's D. russelii revealed 17 PLA 2 isoforms, whereas only four isoforms from Sri Lanka were reported accounting about 32.8% and 35% of total venom protein, respectively . Such disparity in the presence of PLA 2 component in the venom samples appears to support the intraspecies variation in venom composition.…”

Section: Introductionmentioning

confidence: 94%

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

Deka

Sharma

et al. 2017

J Biochem & Molecular Tox

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The present study describes the purification and partial characterization of a basic anticoagulant PLA enzyme named as Rv(i) PLA from the venom of Indian Daboia russelii. The molecular mass of the protein was found to be 13,659.65 Da, and peptide mass fingerprinting revealed that it belongs to group II PLA family. The peptide sequence showed similarity to uncharacterized basic PLA enzyme having an accession no. of P86368 reported from Sri Lankan D. russelii. Rv(i) PLA exhibited strong phospholipase A and anticoagulant activity. It also induced expression of COX-2 and TNF-α mRNA in a dose-dependent manner in phorbol 12-myristate 13-acetate differentiated THP-1 cells, which play a crucial role during inflammation. Chemical modification of His residue in Rv(i) PLA with p-bromophenacyl bromide abolished the enzymatic, anticoagulant, and inflammatory activities. The result indicates that the catalytic site of Rv(i) PLA might play a vital role in inducing inflammation at the bite site during D. russelii envenomation.

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Section: Introductionmentioning

confidence: 94%

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

Deka

Sharma

et al. 2017

J Biochem & Molecular Tox

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“…There is significant variation in the venom composition of Russell's viper in India Figure S9). For example, in one study (Mukherjee et al 2016), VNGF constituted only 0.4% of the venom while in another (Kalita et al 2017), the same protein constituted 4.8% of the venom. As both studies came from the same lab, there is little chance for any technical or assay-related variability.…”

Section: Discussionmentioning

confidence: 94%

“…As both studies came from the same lab, there is little chance for any technical or assay-related variability. In the first study, the venom was used from the captive species in a zoo in the USA where the snake was from a Pakistani origin (Mukherjee et al 2016) while the other study used venom from a commercial source in India (Kalita et al 2017). This suggests that there is a great deal of variation in the composition of Russell's viper venom collected from different locations, corroborating the earlier results (Jayanthi & Gowda 1988;Sharma et al 2015).…”

Section: Discussionmentioning

confidence: 99%

“…The variation in the venom composition within the same species is thought to be a result of adaptation in response to the difference in diets(Barlow et al 2009;Casewell et al 2013; Daltry et al 1996). A comparison across four published studies(Kalita et al 2017;Mukherjee et al 2016;Sharma et al 2015;Tan et al 2015) on Russell's viper venom proteins revealed that the composition of some of the major venom proteins varied significantly (…”

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confidence: 99%

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Peer Review #2 of "Comparative analyses of putative toxin gene homologs from an Old World viper, Daboia russelii (v0.1)"

2017

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Availability of snake genome sequences has opened up exciting areas of research on comparative genomics and gene diversity. One of the challenges in studying snake genomes is the acquisition of biological material from live animals, especially from the venomous ones, making the process cumbersome and time-consuming. Here, we report comparative sequence analyses of putative toxin gene homologs from Russell's viper (Daboia russelii) using whole-genome sequencing data obtained from shed skin. When compared with the major venom proteins in Russell's viper studied previously, we found 45-100% sequence similarity between the venom proteins and their putative homologs in the skin. Additionally, comparative analyses of 20 putative toxin gene family homologs provided evidence of unique sequence motifs in nerve growth factor (NGF), platelet derived growth factor (PDGF), Kunitz/Bovine pancreatic trypsin inhibitor (Kunitz BPTI), cysteine-rich secretory proteins, antigen 5, andpathogenesis-related1 proteins (CAP) and cysteine-rich secretory protein (CRISP). In those derived proteins, we identified V11 and T35 in the NGF domain; F23 and A29 in the PDGF domain; N69, K2 and A5 in the CAP domain; and Q17 in the CRISP domain to be responsible for differences in the largest pockets across the protein domain structures in crotalines, viperines and elapids from the in silico structurebased analysis. Similarly, residues F10, Y11 and E20 appear to play an important role in the protein structures across thekunitzprotein domain of viperids and elapids. Our study highlights the usefulness of shed skin in obtaining good quality high-molecular weight DNA for comparative genomic studies, and provides evidence towards the unique features and evolution of putative venom gene homologs in vipers.

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“…As such, venom components are of wide interest to many research groups and have been the subject of extensive research. As about 90% of venom components are of peptide origin, all venom analyses use increasingly fast developing proteomic techniques, including electrophoresis [8][9][10][11], immunodetection techniques [12][13][14][15], different types of chromatography [16][17][18][19] and mass spectrometry [20][21][22][23]. Each proteomic method has specific requirements for both the sample components and the protein concentration range.…”

Section: Introductionmentioning

confidence: 99%

Comparison of Methods for Measuring Protein Concentration in Venom Samples

Bocian

Sławek

Jaromin

et al. 2020

Animals

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Simple Summary: Snake venom is mostly composed of proteins and peptides, which are of interest to many researchers due to their potential pharmacological properties. Due to their biochemical character, these components are analyzed using proteomic techniques such as electrophoresis, chromatography and mass spectrometry. A very important stage of such studies is the measurement of protein concentration in the sample, which is most often performed by colorimetric methods. In the presented article, we used five such techniques on venoms of two snake species, namely Agkistrodon contortrix and Naja ashei. In the case of A. contortrix venom, four methods provide similar concentration values, whereas, in the case of N. ashei, the differences between results are very significant. The source of these differences should probably be seen in the differences in amino acid composition of proteins of these two venoms. With this report, we would like to draw attention to the need to select an appropriate method for measuring the concentration of protein in the venom, especially in the case of Elapid species.Abstract: Snake venom is an extremely interesting natural mixture of proteins and peptides, characterized by both high diversity and high pharmacological potential. Much attention has been paid to the study of venom composition of different species and also detailed analysis of the properties of individual components. Since proteins and peptides are the active ingredients in venom, rapidly developing proteomic techniques are used to analyze them. During such analyses, one of the routine operations is to measure the protein concentration in the sample. The aim of this study was to compare five methods used to measure protein content in venoms of two snake species: the Viperids representative, Agkistrodon contortrix, and the Elapids representative, Naja ashei. The study showed that for A. contortrix venom, the concentration of venom protein measured by four methods is very similar and only the NanoDrop method clearly stands out from the rest. However, in the case of N. ashei venom, each technique yields significantly different results. We hope that this report will help to draw attention to the problem of measuring protein concentration, especially in such a complex mixture as animal venoms.

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A proteomic analysis of Pakistan Daboia russelii russelii venom and assessment of potency of Indian polyvalent and monovalent antivenom

Cited by 76 publications

References 81 publications

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

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

Peer Review #2 of "Comparative analyses of putative toxin gene homologs from an Old World viper, Daboia russelii (v0.1)"

Comparison of Methods for Measuring Protein Concentration in Venom Samples

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A proteomic analysis of Pakistan Daboia russelii russelii venom and assessment of potency of Indian polyvalent and monovalent antivenom

Cited by 76 publications

References 81 publications

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

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

Peer Review #2 of "Comparative analyses of putative toxin gene homologs from an Old World viper, Daboia russelii (v0.1)"

Comparison of Methods for Measuring Protein Concentration in Venom Samples

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

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