Frontiers in Veterinary Science (May 2024)

The N-glycosylation at positions 652 and 661 of viral spike protein negatively modulates porcine deltacoronavirus entry

  • Hai-Ming Wang,
  • Yang-Yang Qiao,
  • Yong-Gang Liu,
  • Bing-Yan Cai,
  • Yue-Lin Yang,
  • Hui Lu,
  • Yan-Dong Tang,
  • Yan-Dong Tang

DOI
https://doi.org/10.3389/fvets.2024.1430113
Journal volume & issue
Vol. 11

Abstract

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N-glycosylation is a highly conserved glycan modification that plays crucial roles in various physiological processes, including protein folding, trafficking, and signal transduction. Porcine deltacoronavirus (PDCoV) poses a newly emerging threat to the global porcine industry. The spike protein of PDCoV exhibits a high level of N-glycosylation; however, its role in viral infection remains poorly understood. In this study, we applied a lentivirus-based entry reporter system to investigate the role of N-glycosylation on the viral spike protein during PDCoV entry stage. Our findings demonstrate that N-glycosylation at positions 652 and 661 of the viral spike protein significantly reduces the infectivity of PDCoV pseudotyped virus. Overall, our results unveil a novel function of N-glycosylation in PDCoV infection, highlighting its potential for facilitating the development of antiviral strategies.

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