SARS-CoV-2 causes the respiratory syndrome COVID-19 and is responsible for the current pandemic. The S protein of SARS-CoV-2-mediating virus binding to target cells and subsequent viral uptake is extensively glycosylated. Here we focus on how glycosylation of both SARS-CoV-2 and target cells crucially impacts SARS-CoV-2 infection at different levels: (1) virus binding and entry to host cells, with glycosaminoglycans of host cells acting as a necessary co-factor for SARS-CoV-2 infection by interacting with the receptor-binding domain of the SARS-CoV-2 spike glycoprotein, (2) innate and adaptive immune response where glycosylation plays both a protective role and contributes to immune evasion by masking of viral polypeptide epitopes and may add to the cytokine cascade via non-fucosylated IgG, and (3) therapy and vaccination where a monoclonal antibody-neutralizing SARS-CoV-2 was shown to interact also with a distinct glycan epitope on the SARS-CoV-2 spike protein. These evidences highlight the importance of ensuring that glycans are considered when tackling this disease, particularly in the development of vaccines, therapeutic strategies and serological testing.
【저자키워드】 COVID-19, SARS-CoV-2, glycosylation, Infection, Spike protein, Blood group antigen, 【초록키워드】 IgG, vaccination, pandemic, therapy, Vaccines, S protein, glycosylation, SARS-COV-2 infection, monoclonal antibody, spike glycoprotein, cytokine, virus, Spike protein, glycans, immune evasion, Epitopes, Receptor-binding domain, Serological testing, SARS-CoV-2 spike glycoprotein, SARS-CoV-2 spike protein, Impact, Therapeutic strategies, Adaptive immune response, epitope, disease, therapeutic strategy, glycan, monoclonal, binding, Evidence, host cells, target cells, host cell, target cell, Factor, syndrome, protective role, cascade, innate and adaptive immune response, highlight, shown, responsible, subsequent, contribute, the receptor-binding domain, cause, glycosylated, acting, the SARS-CoV-2,