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

## TL;DR

This study shows that specific sugar modifications on a virus's spike protein reduce its ability to infect cells, offering new insights for antiviral strategies.

## Contribution

The novel role of N-glycosylation at positions 652 and 661 in reducing PDCoV infectivity is identified.

## Key findings

- N-glycosylation at positions 652 and 661 of the PDCoV spike protein significantly reduces viral infectivity.
- A lentivirus-based entry reporter system was used to study PDCoV entry mechanisms.
- The findings suggest new potential targets for antiviral strategies against PDCoV.

## Abstract

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.