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

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          Abstract

          To address the dearth of knowledge on the biochemical composition of Pakistan Russell's Viper (Daboia russelii russelii) venom (RVV), the venom proteome has been analyzed and several biochemical and pharmacological properties of the venom were investigated. SDS-PAGE (reduced) analysis indicated that proteins/peptides in the molecular mass range of ~56.0-105.0kDa, 31.6-51.0kDa, 15.6-30.0kDa, 9.0-14.2kDa and 5.6-7.2kDa contribute approximately 9.8%, 12.1%, 13.4%, 34.1% and 30.5%, respectively of Pakistan RVV. Proteomics analysis of gel-filtration peaks of RVV resulted in identification of 75 proteins/peptides which belong to 14 distinct snake venom protein families. Phospholipases A2 (32.8%), Kunitz type serine protease inhibitors (28.4%), and snake venom metalloproteases (21.8%) comprised the majority of Pakistan RVV proteins, while 11 additional families accounted for 6.5-0.2%. Occurrence of aminotransferase, endo-β-glycosidase, and disintegrins is reported for the first time in RVV. Several of RVV proteins/peptides share significant sequence homology across Viperidae subfamilies. Pakistan RVV was well recognized by both the polyvalent (PAV) and monovalent (MAV) antivenom manufactured in India; nonetheless, immunological cross-reactivity determined by ELISA and neutralization of pro-coagulant/anticoagulant activity of RVV and its fractions by MAV surpassed that of PAV.

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          Author and article information

          Journal
          J Proteomics
          Journal of proteomics
          Elsevier BV
          1876-7737
          1874-3919
          Jul 20 2016
          : 144
          Affiliations
          [1 ] Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur, 784028, Assam, India; School of Biological Sciences, University of Northern Colorado, Greeley, CO 80639-0017, USA. Electronic address: akm@tezu.ernet.in.
          [2 ] Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur, 784028, Assam, India.
          [3 ] School of Biological Sciences, University of Northern Colorado, Greeley, CO 80639-0017, USA. Electronic address: stephen.mackessy@unco.edu.
          Article
          S1874-3919(16)30241-X
          10.1016/j.jprot.2016.06.001
          27265321
          b74f672f-62f9-40df-90e7-a68ac9de9872
          History

          ESI-LC-MS/MS,Pro-coagulant,Snake venom enzymes,Snake venom non-enzymatic proteins,Venom-antivenom cross-reactivity,Anticoagulant

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