<i>N</i>-Glycoproteomic Portraits of <i>Bothrops</i> Snake Venoms Reveal Evolutionarily Conserved and Divergent Phenotypes.

ABSTRACT: Glycosylation is a major protein post-translational modification in snake venom proteins and contributes to the diversification of proteomes. In this study, we carried out an in-depth analysis of the glycosylation profile of seven Bothrops venoms, including neutral sugar quantification, glycoprotein profiling by lectin blot, and determination of N-glycosylation sites in proteins and their N-glycan compositions, by direct, intact glycopeptide analysis by mass spectrometry. Interestingly, all identified N-glycosylated peptides were from enzymatic venom components, mainly proteolytic enzymes that are key in envenomation. All venoms revealed a prominent occurrence of fucose and sialic acid in all N-glycosylated toxins identified. The results indicated that in

SUBMITTER: Andrade-Silva D 

PROVIDER: S-EPMC12687316 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature