tetano
Editor, Senior Moderator
mBio
. 2024 Jan 9:e0167223.
doi: 10.1128/mbio.01672-23. Online ahead of print. SARS-CoV-2 spike glycosylation affects function and neutralization sensitivity
Fengwen Zhang[SUP] 1 [/SUP], Fabian Schmidt[SUP] 1 [/SUP], Frauke Muecksch[SUP] 1 [/SUP], Zijun Wang[SUP] 2 [/SUP], Anna Gazumyan[SUP] 2 3 [/SUP], Michel C Nussenzweig[SUP] 2 3 [/SUP], Christian Gaebler[SUP] 2 [/SUP], Marina Caskey[SUP] 2 [/SUP], Theodora Hatziioannou[SUP] 1 [/SUP], Paul D Bieniasz[SUP] 1 3 [/SUP]
Affiliations
The attachment of glycans to the spike proteins of viruses during their synthesis and movement through the secretory pathway can affect their properties. This study shows that the glycans attached to the severe acute respiratory syndrome coronavirus-2 spike protein enable its movement to the cell surface and incorporation into virus particles. Certain glycans, including one that is attached to asparagine 343 in the receptor-binding domain of the spike protein, can also affect virus neutralization by antibodies. This glycan can increase or decrease sensitivity to individual antibodies, likely through direct effects on antibody epitopes and modulation of spike conformation. However, the overall effect of the glycan in the context of the polyclonal mixture of antibodies in convalescent serum is to reduce neutralization sensitivity. Overall, this study highlights the complex effects of glycosylation on spike protein function and immune evasion.
Keywords: SARS-CoV-2; antibody function; glycosylation; neutralization.
. 2024 Jan 9:e0167223.
doi: 10.1128/mbio.01672-23. Online ahead of print. SARS-CoV-2 spike glycosylation affects function and neutralization sensitivity
Fengwen Zhang[SUP] 1 [/SUP], Fabian Schmidt[SUP] 1 [/SUP], Frauke Muecksch[SUP] 1 [/SUP], Zijun Wang[SUP] 2 [/SUP], Anna Gazumyan[SUP] 2 3 [/SUP], Michel C Nussenzweig[SUP] 2 3 [/SUP], Christian Gaebler[SUP] 2 [/SUP], Marina Caskey[SUP] 2 [/SUP], Theodora Hatziioannou[SUP] 1 [/SUP], Paul D Bieniasz[SUP] 1 3 [/SUP]
Affiliations
- PMID: 38193662
- DOI: 10.1128/mbio.01672-23
The attachment of glycans to the spike proteins of viruses during their synthesis and movement through the secretory pathway can affect their properties. This study shows that the glycans attached to the severe acute respiratory syndrome coronavirus-2 spike protein enable its movement to the cell surface and incorporation into virus particles. Certain glycans, including one that is attached to asparagine 343 in the receptor-binding domain of the spike protein, can also affect virus neutralization by antibodies. This glycan can increase or decrease sensitivity to individual antibodies, likely through direct effects on antibody epitopes and modulation of spike conformation. However, the overall effect of the glycan in the context of the polyclonal mixture of antibodies in convalescent serum is to reduce neutralization sensitivity. Overall, this study highlights the complex effects of glycosylation on spike protein function and immune evasion.
Keywords: SARS-CoV-2; antibody function; glycosylation; neutralization.