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Structure and function of N‐glycans in cobra venom glycoproteins: Site specific glycosylation for structural stability and terminal sialic acid for target selection
Author(s) -
Chien Kun Yi,
Wu Wen Guey,
Bui Ba Han,
Lin Chien Chu
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.lb194
Subject(s) - glycan , sialic acid , snake venom , glycosylation , biochemistry , glycoprotein , mannose , biology , chemistry , venom
Snake venoms consist of glycoproteins such as phosphodiesterase (PDE), 5′‐nucleotidase (5NT), L‐amino acid oxidase (LAAO) and snake venom metalloprotease (SVMP) with different degree of glycosylations, but their structures and functions remain largely unknown. We purify these four enzymes from Taiwan cobra ( N. atra ) venoms and determine their respective glycosylation patterns at peptide level using mass spectrometry. Although the detected N ‐glycan structures are diverse with mainly complex and high mannose type, they are found to be site specific. For instance, cobra PDE consists of 7 N ‐glycans with 4 high mannose and 3 complex types without detectable sialic acid. In contrast, K‐like SVMP consists of 2 complex type N ‐glycans with different degree of sialylations. Additional 3D structural and enzymatic characterizations indicate that the high mannose N ‐glycan in PDE maintain the PDE 3D structures while the terminal sialic acid of the complex type glycan in SVMP play a role in target selection of fibrinogen. We conclude that the N ‐glycans of snake venom glycoproteins play both structural and functional roles and likely involve in the action mechanism of venom toxicity. Support or Funding Information MOST, Taiwan This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .