{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7199903","sourcedb":"PMC","sourceid":"7199903","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7199903","text":"Additionally, the processing of complex-type glycans is an important consideration in immunogen engineering, especially considering that epitopes of neutralizing antibodies against SARS-CoV-2 S can contain fucosylated glycans at N343 (35). Across the 22 N-linked glycosylation sites, 52% are fucosylated and 15% of the glycans contain at least one sialic acid residue (table S2 and fig. S3). Our analysis reveals that N343 is highly fucosylated with 98% of detected glycans bearing fucose residues. Glycan modifications can be heavily influenced by the cellular expression system used. We have previously demonstrated for HIV-1 Env glycosylation that the processing of complex-type glycans is driven by the producer cell but that the levels of oligomannose-type glycans were largely independent of the expression system and are much more closely related to the protein structure and glycan density (36).","typesettings":[{"style":"italic","span":{"begin":235,"end":237}},{"style":"italic","span":{"begin":899,"end":901}}]}