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
peer-reviewed · International Journal of Biological Macromolecules · 2020
| Date | 2020-01-23 |
| Type | peer-reviewed |
| Venue | International Journal of Biological Macromolecules |
| Publisher | Elsevier BV |
| Contribution | downstream-application |
| DOI | 10.1016/j.ijbiomac.2020.01.226 |
| Citations (OpenAlex) | 29 |
| Venue 2-year citedness | 8.99 |
Abstract
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 A 2 , 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.
Methods and tools
- Malabar pit viper venomics: Venomics workflow combining SDS-PAGE and ion-exchange pre-fractionation with LC-MS/MS + Novor and PEAKS de novo sequencing to identify 97 proteins (including 18 exclusive to de novo) from Trimeresurus malabaricus venom, and evaluate antivenom cross-reactivity.
Methods it uses
Data deposited
- Proteomics of venom from Trimeresurus malabaricus (as deposited) · PXD011673
Cites (3)
- Mass spectrometry-assisted venom profiling of Hypnale hypnale found in the Western Ghats of India incorporating de novo sequencing approaches (2018) crossref
- DeNovoGUI: An Open Source Graphical User Interface for de Novo Sequencing of Tandem Mass Spectra (2014) crossref
- Charting the Proteomes of Organisms with Unsequenced Genomes by MALDI-Quadrupole Time-of-Flight Mass Spectrometry and BLAST Homology Searching (2001) crossref