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Publications

Journal Article Research Support, Non-U.S. Gov't Ppublish 4 citations

PubMed: 38679392 DOI: 10.1016/j.virusres.2024.199381

The glycosylation sites in RBD of spike protein attenuate the immunogenicity of PEDV AH2012/12.

Virus Res 345:199381

Authors: Gege Zhang, Qi Peng, Shiyu Liu, Baochao Fan, Chuanhong Wang, Xu Song, Qiuxia Cao, Chengcheng Li, Hong Xu, Hongting Lu, Meiying Bao, Shanshan Yang, Yunchuan Li, Jiaxiang Wang, Bin Li

Affiliations

  • College of Animal Science, Yangtze University, Jingzhou 434025, China; Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Nanjing, Jiangsu 210014, China.
  • Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Nanjing, Jiangsu 210014, China.
  • Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Nanjing, Jiangsu 210014, China; College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China; Jiangsu Co-Innovation Center for the Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Jiangsu Key Laboratory of Zoonoses, Yangzhou University, Yangzhou, Jiangsu 225009, China.
  • Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Nanjing, Jiangsu 210014, China; Jiangsu Co-Innovation Center for the Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Jiangsu Key Laboratory of Zoonoses, Yangzhou University, Yangzhou, Jiangsu 225009, China; GuoTai (Taizhou) Center of Technology Innovation for Veterinary Biologicals, Taizhou, Jiangsu 225300, China.
  • College of Animal Science, Yangtze University, Jingzhou 434025, China.
  • Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Nanjing, Jiangsu 210014, China; College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China; Jiangsu Co-Innovation Center for the Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Jiangsu Key Laboratory of Zoonoses, Yangzhou University, Yangzhou, Jiangsu 225009, China; GuoTai (Taizhou) Center of Technology Innovation for Veterinary Biologicals, Taizhou, Jiangsu 225300, China.

Abstract

Porcine epidemic diarrhea (PED) is a highly contagious swine intestinal disease caused by PED virus (PEDV). Vaccination is a promising strategy to prevent and control PED. Previous studies have confirmed that glycosylation could regulate the immunogenicity of viral antigens. In this study, we constructed three recombinant PEDVs which removed the glycosylation sites in RBD. Viral infection assays revealed that similar replication characteristics between the recombinant viruses and parental PEDV. Although animal challenging study demonstrated that the glycosylation sites in RBD do not affect the pathogenicity of PEDV, we found that removing the glycosylation sites on the RBD regions could promote the IgG and neutralization titer in vivo, suggesting deglycosylation in RBD could enhance the immunogenicity of PEDV. These findings demonstrated that removal of the glycosylation sites in RBD is a promising method to develop PEDV vaccines.

MeSH

Vaccines, Virology, Viruses

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