A group from Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control and Prevention (CDC), Atlanta, GA USA etc. has reported on changes in N-glycan profiles between the wild type (S-614D) and the variant (S-614G) SARS-CoV-2.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8651636/
The site-specific distribution and abundance of heterogeneous N-linked glycans on 21 of 22 potential sequons were characterized by mass spectrometry analysis of the glycopeptides cleaved by the a-lytic protease or the combination of trypsin and chymotrypsin.
Analysis of the S-614G variant revealed differences in the N-glycan on some glycosylation sites from those seen in S-614D. Among 21 detected and quantified sequons, 9 of these sequons including N17, N61, N74, N331, N343, N657, N1074, N1158, and N1173 had little to no significant variations in the distribution of both individual glycans and glycan types between S-614D and S-614G protein expressions while alterations were observed on 11 of sequons that include N122, N165, N234, N282, N603, N616, N709, N717, N801, N1098, and N1134.
The relative abundances of the complex-type glycans were reduced by up to 45% on those sequons with altered N-glycosylation in the S-614G glycoprotein and the contents of high-mannose glycans, in contrast, were elevated by up to 33%.