Delineating the venom toxin arsenal of Malabar pit viper (Trimeresurus malabaricus) from the Western Ghats of India and evaluating its immunological cross-reactivity and in vitro cytotoxicity

• Published in: International journal of biological macromolecules Vol. 148; pp. 1029 - 1045
• Main Authors: Vanuopadath, Muralidharan, Shaji, Sanu Korumadathil, Raveendran, Dileepkumar, Nair, Bipin Gopalakrishnan, Nair, Sudarslal Sadasivan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2020
• Subjects: 5'-Nucleotidase - chemistry; Animals; Antivenins - chemistry; Apoptosis - drug effects; Cell Line; Cell Survival - drug effects; Chromatography, High Pressure Liquid; Crotalid Venoms - analysis; Crotalid Venoms - enzymology; Crotalid Venoms - toxicity; Daboia; De novo sequencing; Humans; India; L-Amino Acid Oxidase - chemistry; Lectins, C-Type - chemistry; Malabar pit viper; Mass spectrometry; Metalloproteases - chemistry; Mice; Phospholipases A2 - chemistry; Proteome - chemistry; Serine Proteases - chemistry; Snake venom proteomics; Tandem Mass Spectrometry; Trimeresurus; Trimeresurus malabaricus; India; Malabar pit viper; Trimeresurus malabaricus; De novo sequencing; Snake venom proteomics; Mass spectrometry
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2020.01.226

The venom protein components of Malabar pit viper (Trimeresurus malabaricus) were identified by combining SDS-PAGE and ion-exchange chromatography pre-fractionation techniques with LC-MS/MS incorporating Novor and PEAKS-assisted de novo sequencing strategies. Total 97 proteins that belong to 16 protein families such as L-amino acid oxidase, metalloprotease, serine protease, phospholipase A2, 5′-nucleotidase, C-type lectins/snaclecs and disintegrin were recognized from the venom of a single exemplar species. Of the 97 proteins, eighteen were identified through de novo approaches. Immunological cross-reactivity assessed through ELISA and western blot indicate that the Indian antivenoms binds less effectively to Malabar pit viper venom components compared to that of Russell's viper venom. The in vitro cell viability assays suggest that compared to the normal cells, MPV venom induces concentration dependent cell death in various cancer cells. Moreover, crude venom resulted in chromatin condensation and apoptotic bodies implying the induction of apoptosis. Taken together, the present study enabled in dissecting the venom proteome of Trimeresurus malabaricus and revealed the immuno-cross-reactivity profiles of commercially available Indian polyvalent antivenoms that, in turn, is expected to provide valuable insights on the need in improving antivenom preparations against its bite. •First report on Trimeresurus malabaricus venom proteome.•Total of 97 proteins were identified from the crude venom.•18 proteins were exclusively identified through de novo approaches.•Indian polyvalent antivenoms shows considerable cross-reactivity towards T. malabaricus venom proteins.