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Severe acute respiratory syndrome coronavirus 2 is the causative pathogen of the COVID-19 pandemic which as of January 10, 2021 has claimed 1,926,625 lives worldwide. Vaccine development efforts focus on the viral trimeric spike glycoprotein as the main target of the humoral immune response. Viral spikes carry glycans that facilitate immune evasion by shielding specific protein epitopes from antibody neutralization and antigen efficacy is influenced by spike glycoprotein production in vivo 1. Therefore, immunogen integrity is important for glycoprotein-based vaccine candidates. Here we show how site-specific glycosylation differs between virus-derived spikes, spike proteins derived from a viral vectored SARS-CoV2 vaccine candidate and commonly used recombinant, engineered spike glycoproteins. Furthermore, we show that their distinctive cellular secretion pathways result in different protein glycosylation and secretion patterns, including shedding of spike monomeric subunits for the vaccine candidate tested, which may have implications for the resulting immune response and vaccine design

Type

Journal article

Journal

ACS Central Science

Publisher

American Chemical Society

Publication Date

21/03/2021