Furin cleavage of the SARS-CoV-2 spike is modulated by O-glycosylation

@article{Zhang2021FurinCO,
  title={Furin cleavage of the SARS-CoV-2 spike is modulated by O-glycosylation},
  author={Liping Zhang and Matthew F. Mann and Zulfeqhar A. Syed and Hayley M. Reynolds and E. Tian and Nadine L. Samara and Darryl C. Zeldin and Lawrence A. Tabak and Kelly G. Ten Hagen},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2021},
  volume={118}
}
Significance The novel SARS-CoV-2 coronavirus that is responsible for the global pandemic contains a unique insertion of four amino acids within the spike protein (S). Furin cleavage at this novel insertion site has been shown to increase pseudoviral infectivity and syncytia formation. Here we show that O-glycosylation by certain GALNT family members decreases furin cleavage of S and decreases syncytia formation. Moreover, we show that P681 mutations found in the highly transmissible alpha and… 

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