Determination of Molecular Traces of Various Snake Venomes Using Proteomics and Glycomic Approaches Based on Mass Spectrometry

Abstract

Viperidae snake species are distributed in a wide geographical region in Turkey. Specific proteome and glycoproteome composition profiles provide comprehensive information to study the venom’s biological function and taxonomical classification. In this context, we used proteomics, glycoproteomics, and glycomics strategies to characterize proteins present in the proteome and glycoproteome of five venoms belonging to the Viperidae family. The finding showed a distinct composition for each venom, particularly the glycoproteome profile. The overall mass spectrometry profiles identified 144 different proteins, 36 glycoproteins and 78 distinct N-glycan structures varying in composition across the five venoms. The glycoprotein composition data obtained from glycoproteomics aligns consistently with the findings from glycomics. Many the identified proteins across the five venoms belong to glycosylated protein families, snake venom serine protease (SVSP), snake venom metalloprotease (SVMP), and C-type lectins (CTL). The clustering and principal component analyses (PCA) illustrated the composition-based similarities and differences between venom proteome, glycoproteome and glycan profiles. Specifically, the N-glycan profiles of M. xanthina (Mx) and V. a. ammodytes (Vaa) venoms were identical and difficult to differentiate; in contrast, their proteome profiles were distinct. Clustering analysis enabled the classification of venom species into different groups presenting their taxonomical classification. Interestingly, the variety of the proteins across venom species highlights the impact of glycosylation on the diversity of glycosylated protein in venom proteome. This proposed high throughput approach provides accurate and comprehensive profiles of the composition and function of various Viperidae snake venoms.