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

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

JOURNAL=Frontiers in Veterinary Science

VOLUME=11

YEAR=2024

URL=https://www.frontiersin.org/journals/veterinary-science/articles/10.3389/fvets.2024.1430113

DOI=10.3389/fvets.2024.1430113

ISSN=2297-1769

ABSTRACT=<p><italic>N</italic>-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 <italic>N</italic>-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 <italic>N</italic>-glycosylation on the viral spike protein during PDCoV entry stage. Our findings demonstrate that <italic>N</italic>-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 <italic>N</italic>-glycosylation in PDCoV infection, highlighting its potential for facilitating the development of antiviral strategies.</p>