Identification of Snake Venoms According to their Protein Content Using the MALDI-TOF-MS Method

Snakebites cause mortality and morbidity in tropical regions. Bites by Viperidae and Elapidae family snakes are common in Turkey. Snake venom characterization and anti-venom production are important in the diagnosis and treatment of snakebites. Our objective was to develop a method for analyzing all venoms by identifying basic protein structures in venom using a MALDI-TOF-MS and to create a venom library. Five Viperidae family and one from the Elapidae family venoms, were identified. Although the proportions vary depending on the species and subspecies, the identification procedure involved determining the protein structures of PLA2, VEGF, svMP, CRISP, svSP, PIII-MP, and LAAO, common to all venoms. Six matrices (CHCA, DHAP, DHB, SA, S-DHB and THAP,) with the MALDI-TOF-MS and six snake venoms were studied separately. On the other hand, peptide profiles were studied in the mass range of 1000-10000 Da using reflectron mode. It was found that biomarkers peptides were 4398, 4026, 6395, 3800 and 6672 Da for ML, MX, VAA, VBB, VAM and WA respectively. The highest relative abundance values of the protein signals were mostly obtained with both the CHCA and the DHAP matrices. Some targeted protein structures were not observed in studies involving the S-DHB and the THAP matrices, and those were detected exhibited relatively low abundance.