Project description:Porcine epidemic diarrhea (PED) is an acute, highly contagious, and high-mortality enterophilic infectious disease caused by the porcine epidemic diarrhea virus (PEDV). PEDV is globally endemic and causes substantial economic losses in the swine industry. The PEDV E protein is the smallest structural protein with high expression levels that interacts with the M protein and participates in virus assembly. However, how the host proteins interact with E proteins in PEDV replication remains unknown. We identified host proteins that interact with the PEDV E protein using a combination of PEDV E protein-labeled antibody co-immunoprecipitation and tandem liquid-chromatography mass-spectroscopy (LC-MS/MS).
Project description:Porcine epidemic diarrhea (PED), caused by porcine epidemic diarrhea virus (PEDV), is an acute and contagious enteric disease with high mortality in sucking piglets, causing huge economic losses to swine industry. In this study, we used tandem mass tag (TMT) quantitative protein analysis to investigate the proteomic changes of PK15 cells after PEDV infection, and the differential protein expression profiles were obtained at 0 h, 24 h, and 48 h after PEDV infection
Project description:The spike protein of the porcine epidemic diarrhea virus from various strains was generated from different mammalian expression systems. The integration of cryo-EM and MS delineated the glycosylation patterns on Spike proteins and also helped understand how individual glycans contribute to biological functions.
Project description:Porcine epidemic diarrhea virus (PEDV) is a highly pathogenic infectious disease targeting pig intestine that is widespread in the world, causing huge economic losses to pig industry. PEDV N protein is the core protein of PEDV, which locates in the cytoplasm and wraps the RNA genome of the virus to form spiral ribonucleoprotein (RNP). However, host proteins interacting with N proteins and their role in PEDV replication have not been fully elucidated. In this study, PEDV-N labeled antibodies were immunoprecipitated (Co-IP) and combined with LC-MS/MS to screen host proteins interacting with N proteins.
