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[C. Omics & Fusion Biology] C-4

Mouse Brain N-Glycome DB: Investigation of brain region-

specific N-glycome diversity using nanoLC-MS/MS

Dongtan Yin¹,², Hee Young Jo¹,², Hyun Joo An¹,²*

¹Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon 34134, Korea,

²Asia-pacific Glycomics Reference Site, Chungnam National University, Daejeon 34134, Korea

In the mammalian brain, over 70% of proteome is known to be glycosylated, and a large fraction of the glycosylation

is N-glycome. Protein N-glycosylation plays an important role in neuro-biological, including neural development,
and neurotransmitter receptor regulation. However, our current understanding of N-glycome for exploring brain

biological function remains largely limited due to structurally complexity and heterogeneity. To facilitate brain
glycosylation studies, we built a glycome database using PGC nanoLC-MS/MS, an isomer-sensitive and reproducible

glycan analysis platform. In detail, putative brain glycan structures were elucidated by considering diagnostic
fragment peaks in MS/MS and RT together. A total of 130 N-glycans were found in brain including 44 glycans (~90%

NAPI), detected in all brain samples. Interestingly, the major 44 N-glycans exhibited unique glycomic characteristics
of the brain, consisting predominantly of high-mannose and fucosylated/bisected glycans. In addition, at least 87

N-glycans such as bisected/sialylated hybride type, sialylated LacdiNAc/HexNAc, outer fucosylated glycans with
sialylated HexNAc, highly branched and fucosylated, and Lewis Y(B) contributed to the diversity of brain region-

speicfic N-glycome, A total of 130 N-glycans, including structural information of glyco biosynthesis, were entered
into the database for each brain region. This will be used as an excellent resource for brain glycome research.