Abstract The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323.
【저자키워드】 SARS-CoV-2, mass spectrometry, spike glycoprotein, glycoproteomics, 【초록키워드】 COVID-19, glycosylation, spike glycoprotein, angiotensin-converting enzyme 2, Novel coronavirus, Receptor-binding domain, glycoprotein, Interaction, angiotensin, N-glycan, infective agent, human disease, infection process, novel coronavirus SARS-CoV-2, receptor-binding domains, human cell, the receptor-binding domain, glycosylated, 【제목키워드】 spike glycoprotein, SARS-CoV-2 spike glycoprotein, domain,