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A Brief Appraisal on Russell’s Viper Venom (Daboia russelii russelii) Proteinases

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Snake Venoms

Part of the book series: Toxinology ((TOXI))

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Abstract

Russell’s viper (Daboia russelii) is an important member of the Viperidae family which is widely distributed across Southern Asia including India. Russell’s viper venom (RVV) is indisputably a potent mixture of various toxic and nontoxic components that have evolved to interfere with vital physiological processes like coagulation and fibrinolysis. Many of these components are metallo- or serine proteinases. Venoms from the snakes of Viperidae family are reported to be rich in proteinases which contributes to hemostatic alterations in the victims and is also responsible for tissue-specific hemorrhagic effects. However, till date, not many proteinases have been reported from RVV. In this brief review, the currently available data on the structural and functional attributes of RVV proteinases have been focused and summarized. The pathophysiological significance and the therapeutic/ diagnostic application(s) of the identified RVV proteinases have also been discussed. It is relevant to note that a more detailed analysis of the entire complexity of RVV proteinases will contribute to the better understanding of their role in Russell’s viper envenomation and subsequent antivenom therapy. Most importantly, novel RVV proteinases can also be explored for their usefulness in the development of diagnostic/therapeutic agents to deal with life-threatening diseases.

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References

  • Amiconi G, Amoresano A, Boumis G, Brancaccio A, De Cristofaro R, De Pascalis A, Di Girolamo S, Maras B, Scaloni A. A novel venombin B from Agkistrodon contortrix contortrix: evidence for recognition properties in the surface around the primary specificity pocket different from thrombin. Biochemistry. 2000;39:10294–308.

    Article  CAS  PubMed  Google Scholar 

  • Barrett AJ, Rawlings ND. Families and clans of serine peptidases. Arch Biochem Biophys. 1995;318:247–50.

    Article  CAS  PubMed  Google Scholar 

  • Bjarnason JB, Fox JW. Hemorrhagic metalloproteinases from snake venoms. Pharmacol Ther. 1994;62:325–72.

    Article  CAS  PubMed  Google Scholar 

  • Bode W, Gomis-Ruth FX, Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the “metzincins”. FEBS Lett. 1993;331:134–40.

    Article  CAS  PubMed  Google Scholar 

  • Chakrabarty D, Bhattacharya D, Sarkar HS, Lahiri SC. Purification and partial characterization of a haemorrhagin (VRH-I) from Vipera russelli russelli venom. Toxicon. 1993;31:1601–14.

    Article  CAS  PubMed  Google Scholar 

  • Chakrabarty D, Datta K, Gomes A, Bhattacharyya D. Haemorrhagic protein of Russell’s Viper venom with fibrinolytic and esterolytic activities. Toxicon. 2000;38:1475–90.

    Article  CAS  PubMed  Google Scholar 

  • Chen H-S, Tsai H-Y, Wang Y-M, Tsai I-H. P-III hemorrhagic metalloproteinases from Russell’s Viper venom: cloning, characterization, phylogenetic and functional site analyses. Biochimie. 2008;90:1486–98.

    Article  CAS  PubMed  Google Scholar 

  • Deshimaru M, Ogawa T, Nakashima K, Nobuhisa I, Chijiwa T, Shimohigashi Y, Fukumaki Y, Niwa M, Yamashina I, Hattori S, Ohno M. Accelerated evolution of crotalinae snake venom gland serine proteinases. FEBS Lett. 1996;397:83–8.

    Article  CAS  PubMed  Google Scholar 

  • Faiz MA, Falkous G, Harris JB, Mantle D. Comparison of proteinase and related enzyme activities in snake venoms. Comp Biochem Physiol B. 1996;113:199–204.

    Article  CAS  PubMed  Google Scholar 

  • Fox JW, Serrano SMT. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon. 2005;45:969–85.

    Article  CAS  PubMed  Google Scholar 

  • Fox JW, Serrano SMT. Timeline of key events in snake venom metalloproteinase research. J Proteomics. 2009;72:200–9.

    Article  CAS  PubMed  Google Scholar 

  • Furie BC, Furie B. Coagulant protein of Russell’s Viper venom. In: Lorand L, editor. Methods of enzymology. San Diego: Academic; 1976.

    Google Scholar 

  • Furie BC, Furie B, Gottliels AJ, Williams WJ. Activation of bovine factor X by the venom coagulant protein of Vipera russelli: complex formation of the activation fragments. Biochim Biophys Acta. 1974;365:121–32.

    Article  CAS  PubMed  Google Scholar 

  • Furukawa K, Ishimaru S. Use of thrombin-like snake venom enzymes in the treatment of vascular occlusive diseases. In: Stocker KF, editor. Medical use of snake venom proteins. Boca Raton: CRC Press; 1990.

    Google Scholar 

  • Gowda DC, Jackson CM, Hensley P, Davidson EA. Factor-X activating glycoprotein of Russell’s Viper venom-polypeptide composition and characterization of the carbohydrate moieties. J Biol Chem. 1994;269:10644–50.

    CAS  PubMed  Google Scholar 

  • Gutierrez JM, Rucavado A. Snake venoms metalloproteinases: their role in the pathogenesis of local tissue damage. Biochimie. 2000;82:841–50.

    Article  CAS  PubMed  Google Scholar 

  • Hite LA, Jia LG, Bjarnason JB, Fox JW. cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins. Arch Biochem Biophys. 1994;308:182–91.

    Article  CAS  PubMed  Google Scholar 

  • Howes JM, Kamiguti AS, Theakston RDG, Wilkinson MC, Laing GD. Effects of three novel metalloproteinases from the venom of the West African saw-scaled Viper, Echis ocellatus on blood coagulation and platelets. Biochim Biophys Acta. 2005;1724:194–202.

    Article  CAS  PubMed  Google Scholar 

  • Itoh N, Tanaka N, Mihashi S, Yamashina I. Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin-like snake venom enzyme. J Biol Chem 1987; 262: 3132–3135.

    CAS  PubMed  Google Scholar 

  • Jayanthi GP, Gowda TV. Geographical variation in India in the composition and lethal potency of Russell’s Viper (Vipera russelli) venom. Toxicon. 1988;26:257–64.

    Article  CAS  PubMed  Google Scholar 

  • Jayanthi GP, Gowda TV. Synergistic interaction of a proteinase and proteinase inhibitors from Russell’s Viper (Vipera russelli) venom. Toxicon. 1990;28(1):65–74.

    Article  CAS  PubMed  Google Scholar 

  • Jy WC, Horstman LL, Wang F, Duncan RC, Ahn YS. Platelet factor 3 in plasma fractions – its relation to micro- particle size and thromboses. Thromb Res. 1995;80:471–82.

    Article  CAS  PubMed  Google Scholar 

  • Kasturi S, Gowda TV. Purification and characterization of a major phospholipase A2 from Russell’s Viper (Vipera russelii) venom. Toxicon. 1988;27:229–37.

    Article  Google Scholar 

  • Kasturiratne A, Wickremasinghe R, de Silva N, Gunawardena NK, Pathmeswaran A, Premaratna R, Savioli L, Lalloo DG, de Silva HJ. The global burden of snakebite: a literature analysis and modelling based on regional estimates of envenoming and deaths. PLoS Med. 2008;5:e218.

    Article  PubMed  PubMed Central  Google Scholar 

  • Kini RM. The intriguing world of prothrombin activators from snake venom. Toxicon. 2005;45:1133–45.

    Article  CAS  PubMed  Google Scholar 

  • Kisiel W. Molecular properties of the factor V-activating enzyme from Russell’s Viper venom. J Biol Chem. 1979;254:12230–4.

    CAS  PubMed  Google Scholar 

  • Kisiel W, Canfield WM. Snake venom proteinases that activate blood coagulation factor V. In: Lorand L, editor. Methods in enzymology. New York: Academic; 1981.

    Google Scholar 

  • Kisiel W, Hermodson MA, Davie EW. Factor X activating enzyme from Russell’s Viper venom: isolation and characterization. Biochemistry. 1976;15:4901–6.

    Article  CAS  PubMed  Google Scholar 

  • Markland FS. Snake venoms and the hemostatic system. Toxicon. 1998;36:1749–800.

    Article  CAS  PubMed  Google Scholar 

  • Marrakchi N, Barbouche R, Guermazi S, Karoui H, Bon C, Eiayeb M. Cerastotin, a serine protease from Cerastes cerastes venom, with platelet-aggregating and agglutinating properties. Eur J Biochem. 1997;247:121–8.

    Article  CAS  PubMed  Google Scholar 

  • Marsh N, Williams V. Practical applications of snake venom toxins in haemostasis. Toxicon. 2005;45:1171–81.

    Article  CAS  PubMed  Google Scholar 

  • Matsui T, Fujimura Y, Titani K. Snake venom proteinases affecting hemostasis and thrombosis. Biochim Biophys Acta. 2000;1477:146–56.

    Article  CAS  PubMed  Google Scholar 

  • Meier J, Stocker KF. Biology and distribution of venomous snakes of medical importance and the composition of snake venoms. In: Meier J, White J, editors. Handbook of clinical toxicology of animal venoms and poisons. Boca Raton: CRC Press; 1995.

    Google Scholar 

  • Monteiro FNP, Kanchan T, Bhagavath P, Kumar GP, Menezes RG, Yoganarashima J. Clinico-epidemiological features of Viper bite envenomation: a study from Manipal, South India. Singapore Med J. 2012;53(3):203.

    CAS  PubMed  Google Scholar 

  • Moura-da-Silva AM, Furlan MS, Caporrino MS, Grego KF, Portes-Junior JA, Clissa PB, Valente HR, Magalhães GS. Diversity of metalloproteinases in Bothrops neuwiedi snake venom transcripts: evidences for recombination between different classes of SVMPs. BMC Genet. 2011;12:94.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Mukherjee AK. Characterization of a novel pro-coagulant metalloproteinase (RVBCMP) possessing alpha-fibrinogenase and tissue haemorrhagic activity from venom of Daboia russelli russelli (Russell’s Viper): evidence of distinct coagulant and haemorrhagic sites in RVBCMP. Toxicon. 2008;51(5):923–33.

    Article  CAS  PubMed  Google Scholar 

  • Mukherjee AK. The pro-coagulant fibrinogenolytic serine protease isoenzymes purified from Daboia russelii russelii venom coagulate the blood through factor V activation: role of glycosylation on enzymatic activity. PLoS One. 2014;9(2):e86823.

    Article  PubMed  PubMed Central  Google Scholar 

  • Mukherjee AK, Mackessy SP. Russelobin, a non-toxic thrombin-like serine proteinase from the venom of Russell’s Viper (Daboia russelli russelli): possible applications in cardiovascular drug development. Toxicon. 2012;60:109–10.

    Article  CAS  Google Scholar 

  • Mukherjee AK, Mackessy SP. Biochemical and pharmacological properties of a new thrombin-like serine proteinase (Russelobin) from the venom of Russell’s Viper (Daboia russelii russelii) and assessment of its therapeutic potential. Biochim Biophys Acta Gen Sub. 2013;1830:3476–88.

    Article  CAS  Google Scholar 

  • Mukherjee AK, Ghosal SK, Maity CR. Some biochemical properties of Russell’s Viper (Daboia russelli) venom from Eastern India : correlation with clinico-pathological manifestation in Russell’s Viper bite. Toxicon. 2000;38:163–75.

    Article  CAS  Google Scholar 

  • Nakayama D, Ben Y, Miyata T, Takeda S. Structural basis of coagulation factor V recognition for cleavage by RVV-V. FEBS Lett. 2011;585:3020–5.

    Article  CAS  PubMed  Google Scholar 

  • Prasad BN, Uma B, Bhatt SG, Gowda VT. Comparative characterization of Russell’s Viper (Daboia/Vipera russelli) venoms from different regions of the Indian peninsula. Biochim Biophys Acta. 1999;1428:121–36.

    Article  CAS  PubMed  Google Scholar 

  • Quick AJ. Thromboplastin generation: effect of the Bell-Alton reagent and Russell’s Viper venom on prothrombin consumption. Am J Clin Pathol. 1971;55:555–60.

    Article  CAS  PubMed  Google Scholar 

  • Rawlings ND, Barrett AJ, Bateman A. MEROPS: the peptidase database. Nucleic Acids Res. 2010;38:D227–33.

    Article  CAS  PubMed  Google Scholar 

  • Segers K, Rosing J, Nicolaes GAF. Structural models of the snake venom factor V activators from Daboia russelli and Daboia lebetina. Proteins. 2006;64:968–84.

    Article  CAS  PubMed  Google Scholar 

  • Serrano SM, Maroun RC. Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved. Toxicon. 2005;45:1115–32.

    Article  CAS  PubMed  Google Scholar 

  • Shen H-B, Chow K-C. Identification of proteinases and their types. Anal Biochem. 2009;385:153–60.

    Article  CAS  PubMed  Google Scholar 

  • Suntravat M, Yusuksawad M, Sereemaspun A, Pérez JC, Nuchprayoon I. Effect of purified Russell’s Viper venom-factor X activator (RVV-X) on renal hemodynamics, renal functions, and coagulopathy in rats. Toxicon. 2011;58:230–8.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Suwansrinon K, Khow O, Mitmoonpitak C, Daviratanasilpa S, Chaiyabutr N, Sitprija V. Effects of Russell’s Viper venom fractions on systemic and renal hemodynamics. Toxicon. 2007;49:82–8.

    Article  CAS  PubMed  Google Scholar 

  • Suzuki K, Dahlback B, Stenflo J. Thrombin-catalyzed activation of human coagulation factor V. J Biol Chem. 1982;257:6556–64.

    CAS  PubMed  Google Scholar 

  • Takeda S, Igarashi T, Mori H. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases. FEBS Lett. 2007;581:5859–64.

    Article  CAS  PubMed  Google Scholar 

  • Takeda S, Takeya H, Iwanaga S. Snake venom metalloproteinases: structure, function and relevance to the mammalian ADAM/ADAMTS family proteins. Biochim Biophys Acta. 2012;1824:164–76.

    Article  CAS  PubMed  Google Scholar 

  • Takeya H, Nishida S, Miyata T, Kawada S, Saisaka Y, Morita T, Iwanaga S. Coagulation factor X activating enzyme from Russell’s Viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains. J Biol Chem. 1992;267:14109–17.

    CAS  PubMed  Google Scholar 

  • Thiagarajan P, Pengo V, Shapiro SS. The use of dilute Russell Viper venom time for the diagnosis of lupus coagulants. Blood. 1986;68:869–74.

    CAS  PubMed  Google Scholar 

  • Thorpe RS, Pook CE, Malhotra A. Phylogeography of the Russell’s Viper (Daboia russelii) complex in relation to variation in the colour pattern and symptoms of envenoming. Herpetol J. 2007;17:209–18.

    Google Scholar 

  • Tokunaga F, Nagasawa K, Miyata T, Iwanaga S. The factor V-activating enzyme (RVV-V) from Russell’s Viper Venom. J Biol Chem. 1988;263:17471–81.

    CAS  PubMed  Google Scholar 

  • Warrell DA. Snake venoms in science and clinical medicine. 1. Russell’s Viper: biology, venom and treatment of bites. Trans R Soc Trop Med Hyg. 1989;83:732–40.

    Article  CAS  PubMed  Google Scholar 

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Authors and Affiliations

  1. Department of Molecular Biology and Biotechnology, Research and Development, ONGC-Centre for Petroleum Biotechnology, DBT Nodal Centre for Medical Colleges and Biomedical Research Institutes of North-East India (Unit of Department of Biotechnology, Govt. of India), Tezpur University, Tezpur, 784 028, Assam, India

    Ashis K. Mukherjee

  2. Microbial Biotechnology and Protein Research Laboratory, Department of Molecular Biology and Biotechnology, School of Sciences, Tezpur University, Tezpur, 784 028, Assam, India

    Rupamoni Thakur

Authors
  1. Rupamoni Thakur
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  2. Ashis K. Mukherjee
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Correspondence to Ashis K. Mukherjee .

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Editors and Affiliations

  1. Biomedical Research Institute National Institute of Advanced Industria, Tsukuba, Ibaraki, Japan

    Hidetoshi Inagaki

  2. University of Hawaii Cancer Center, Honolulu, Hawaii, USA

    Carl-Wilhelm Vogel

  3. Department of Molecular Biology and Biot, Tezpur University, Tezpur, Assam, India

    Ashis K. Mukherjee

  4. Egyptian Society of Natural Toxins and Z, Faculty of Science Suez Canal University, Ismailia, Egypt

    Tarek R. Rahmy

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Thakur, R., Mukherjee, A.K. (2017). A Brief Appraisal on Russell’s Viper Venom (Daboia russelii russelii) Proteinases. In: Inagaki, H., Vogel, CW., Mukherjee, A., Rahmy, T. (eds) Snake Venoms. Toxinology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6410-1_19

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