Fig. 3: N-glycosylation of HKU1 HE. | Nature Communications

Fig. 3: N-glycosylation of HKU1 HE.

From: Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans

Fig. 3: N-glycosylation of HKU1 HE.The alt text for this image may have been generated using AI.

a Glycoproteomic analysis of N-linked glycosylation in HKU1 HE. Top panel enumerates the total of unique glycan compositions identified per site. Bottom three panels show semiquantitative analyses from extracted peak areas of site-specific N-glycosylation by glycan type (non-glycosylated, high-mannose, hybrid, or complex), fucosylation, and sialylation. Error bars represent the standard deviation of the duplicate measurement. The selected protease dataset from which the data was extracted is indicated for each site: TR trypsin, CH chymotrypsin, AP alpha-lytic protease. A full overview is presented in Supplementary Fig. 9 and Supplementary Data 1. b Surface representation of the dimeric HKU1 HE atomic model, with modelled N-glycans shown as spheres and coloured according to the predominant glycan type shown in (a). c EM density (blue mesh) zoned 2 Å around each of the modelled N-glycans and analogous region for N168. The occupancy and glycan length distribution from glycoproteomics analysis for each site is shown below.

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