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Poster Presentations
Day 2, June 23（Mon.）
Room P (Maesato East, Foyer, Ocean Wing)
- 2P-PM-51
Probing single-molecule protein glycosylation and its structural impact using PTR-based native mass spectrometry
(1IBC, Academia Sinica, 2IBS, NTU)
oHsin-Yung Yen1,2, Ning-En Chang1, Guan-Ting Lian1,2, Yi-An Chen1, Yu-Xi Tsai1, Kay-Hooi Khoo1,2, Shang-Te Hsu1,2
Protein glycosylation is essential for various biological processes and has significant implications in health and disease. However, characterizing glycoproteins, particularly those exhibiting tremendous heterogeneity due to varieties of glycan structures and glycosylation sites, remains as an intractable task. In this study, we present a novel workflow utilizing proton-transfer-reaction mass spectrometry (PTR-MS) to unveil the multilayer complexity of glycosylation of N-Cadherin—a membrane protein crucial for cell-cell adhesion and highly implicated in cancer metastasis. By advancing data-independent acquisition (DIA) approach, more than a thousand of glycoproteoforms of N-Cadherin were identified. Following the combinatorial strategies, such as glycomics, glycoproteomics and in silico computations, we are able to reveal the glycosylation landscape of intact N-Cadherin and unexpectedly discovered its O-mannosylation. Intriguingly, we observed the unique glycosylation patterns of N-Cadherin in two different conformational states, suggesting the function of glycosylation in modulating protein structures. Overall our findings demonstrate the utility of PTR-MS in resolving proteoform-level diversity of glycoprotein and how it brings a new insight into the structural and functional impact of protein glycosylation.