title: Proteomic comparison of Hypnale hypnale (hump-nosed pit-viper) and Calloselasma rhodostoma (Malayan pit-viper) venoms.
abstract: Treatment of Hypnale hypnale bites with commercial antivenoms, even those raised against its sister taxon Calloselasma rhodostoma, has never been clinically successful. As these two genera have been separated for 20million years, we tested to see whether significant variations in venom had accumulated during this long period of evolutionary divergence, and thus could be responsible for the failure of antivenom. Proteomic analyses of C. rhodostoma and H. hypnale venom were performed using 1D and 2D PAGE as well as 2D-DIGE. C. rhodostoma venom was diverse containing large amounts of Disintegrin, Kallikrein, l-amino acid oxidase, Lectin, phospholipase A2 (acidic, basic and neutral) and Snake Venom Metalloprotease. In contrast, while H. hypnale also contained a wide range of toxin types, the venom was overwhelmingly dominated by two molecular weight forms of basic PLA2. 2D-DIGE (2-D Fluorescence Difference Gel Electrophoresis analysis) showed that even when a particular toxin class was shared between the two venoms, there were significant molecular weights or isoelectric point differences. This proteomic difference explains the past treatment failures with C. rhodostoma antivenom and highlights the need for a H. hypnale specific antivenom.
  
  
  CONCLUSIONS
  These results have direct implications for the treatment of envenomed patients in Sri Lanka. The unusual venom profile of Hypnale hypnale underscores the biodiscovery potential of novel snake venoms.
authors.affiliation: Venom Evolution Lab, School of Biological Sciences, University of Queensland, St Lucia, Qld 4072 Australia; Institute for Molecular Biosciences, University of Queensland, St Lucia, Qld 4072 Australia; HEJ Research Institute of Chemistry, International Centre for Chemical and Biological Sciences (ICCBS), University of Karachi, Karachi 75270, Pakistan.
authors.forename: Syed A
authors.initials: SA
authors.lastname: Ali
authors.forename: Kate
authors.initials: K
authors.lastname: Baumann
authors.forename: Timothy N W
authors.initials: TN
authors.lastname: Jackson
authors.forename: Kelly
authors.initials: K
authors.lastname: Wood
authors.forename: Steven
authors.initials: S
authors.lastname: Mason
authors.forename: Eivind A B
authors.initials: EA
authors.lastname: Undheim
authors.forename: Amanda
authors.initials: A
authors.lastname: Nouwens
authors.forename: Ivan
authors.initials: I
authors.lastname: Koludarov
authors.forename: Iwan
authors.initials: I
authors.lastname: Hendrikx
authors.forename: Alun
authors.initials: A
authors.lastname: Jones
authors.forename: Bryan Grieg
authors.initials: BG
authors.lastname: Fry
mesh_terms: D000818:Animals; D000997:Antivenins / Q000737:chemistry; D019143:Evolution, Molecular; D005786:Gene Expression Regulation; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics; D013045:Species Specificity; D014757:Viper Venoms / Q000378:metabolism*; D017819:Viperidae / Q000378:metabolism*
chemical_list: D000997:Antivenins; D020543:Proteome; D014757:Viper Venoms
keywords: 2D gel DiGE; Antivenom; Mass spectrometry; Proteomics; Venom