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The  N-  glycosylation at positions 652 and 661 of viral spike protein negatively modulates porcine deltacoronavirus entry.Front Vet Sci.2024 May 30:11:1430113.doi: 10.3389/fvets.2024.1430113. eCollection 2024

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


Front Vet Sci.2024 May 30:11:1430113.doi: 10.3389/fvets.2024.1430113. eCollection 2024.


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.


Keywords: N-glycosylation; PDCoV; entry; pseudotyped virus; spike protein.


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