Viruses can evade the host immune system by displaying numerous glycans on their surface "spike-proteins" that cover immune epitopes. We have developed an ultrasensitive "single pot" method to assess glycan occupancy and the extent of glycan processing from high-mannose to complex forms at each N-glycosylation site. Though aimed at characterizing glycosylation of viral spike proteins as potential vaccines, this method is applicable for analysis of site-specific glycosylation of any glycoprotein.
[doi:10.25345/C5MJ8N]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Proteinase K ; N-glycan ; heterogeneity ; HIV ; BG505 ; Env ; viral spike ; endoglycosidase
Principal Investigators: (in alphabetical order) |
John R. Yates III, The Scripps Research Institute, USA |
Submitting User: | sbaboo |
Baboo S, Diedrich JK, MartÃnez-Bartolomé S, Wang X, Schiffner T, Groschel B, Schief WR, Paulson JC, Yates JR.
DeGlyPHER: An Ultrasensitive Method for the Analysis of Viral Spike N-Glycoforms.
Anal Chem. 2021 Oct 12;93(40):13651-13657. Epub 2021 Oct 1.
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