MassIVE MSV000087414

Partial Public PXD025990

An ultrasensitive method for analysis of viral spike N-glycoforms

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Description

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

Contact

Principal Investigators:
(in alphabetical order) 		John R. Yates III, The Scripps Research Institute, USA
Submitting User: sbaboo

Publications

Baboo S, Diedrich JK, Martínez-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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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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