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



The study establishes the proteome profile of the Pakistan RVV, thereby indicating the presence of diverse proteins and peptides that play a significant role in the pathophysiology of RVV bite. Further, the proteomic findings will contribute to understand the variation in venom composition owing to different geographical location and identification of pharmacologically important proteins in Pakistan RVV.
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.
Ashis K
AK
Mukherjee
Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur, 784028, Assam, India.
Bhargab
B
Kalita
School of Biological Sciences, University of Northern Colorado, Greeley, CO 80639-0017, USA. Electronic address: stephen.mackessy@unco.edu.
Stephen P
SP
Mackessy
D000818:Animals; D000997:Antivenins / Q000494:pharmacology*; D019483:Disintegrins / Q000032:analysis; D006026:Glycoside Hydrolases / Q000032:analysis; D007194:India; D045726:Metalloproteases / Q000032:analysis; D010154:Pakistan; D054467:Phospholipases A2 / Q000032:analysis; D020543:Proteome / Q000032:analysis*; D040901:Proteomics / Q000379:methods*; D017840:Daboia; D017385:Sequence Homology; D015842:Serine Proteinase Inhibitors / Q000032:analysis; D000637:Transaminases / Q000032:analysis; D014757:Viper Venoms / Q000032:analysis* / Q000737:chemistry
D000997:Antivenins; D019483:Disintegrins; D020543:Proteome; D015842:Serine Proteinase Inhibitors; D014757:Viper Venoms; D000637:Transaminases; D054467:Phospholipases A2; D006026:Glycoside Hydrolases; D045726:Metalloproteases
Anticoagulant; ESI-LC-MS/MS; Pro-coagulant; Snake venom enzymes; Snake venom non-enzymatic proteins; Venom-antivenom cross-reactivity