O‐glycosylation of the novel SARS‐CoV‐2 coronavirus spike protein influences furin cleavage
| Autor: | Lawrence A. Tabak, Darryl C. Zeldin, Hayley M Reynolds, Negin P. Martin, Matthew Mann, Nadine L. Samara, E Tian, Liping Zhang, Kelly G. Ten Hagen, Zulfeqhar Syed |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Infectivity
Syncytium Glycosylation animal structures biology viruses Biochemistry and Molecular Biology virus diseases Cleavage (embryo) medicine.disease_cause Biochemistry Virus Cell biology carbohydrates (lipids) chemistry.chemical_compound chemistry Glycobiology: Analysis and Physiology Genetics biology.protein medicine Molecular Biology Furin Tropism Biotechnology Coronavirus |
| Zdroj: | The FASEB Journal |
| ISSN: | 1530-6860 0892-6638 |
| Popis: | Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the pandemic that has affected millions of people worldwide. This virus contains a unique polybasic insertion (PRRA) within the spike protein, resulting in a novel furin cleavage site that has been shown to influence viral infectivity and syncytia formation in cell culture. This insertion also generates novel putative sites of O-glycosylation, a protein modification that has been shown in other proteins to influence furin cleavage. Here, we define the specific members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GALNT) family that are capable of glycosylating the novel SARS-CoV-2 coronavirus spike and examine their presence in human respiratory cells that are targets for SARS-CoV-2 infection. Moreover, we show that O-glycosylation by specific members of the GALNT enzyme family modulates furin cleavage of the spike in vivo. Given the well-established role of O-glycosylation in the regulation of proteolysis, our results suggest that O-glycosylation of SARS-CoV-2 may play roles in aspects of spike stability/processing, which may influence viral infectivity and tropism. |
| Databáze: | OpenAIRE |
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