Surface Displayed Expression of a Neutralizing Epitope of Spike Protein from a Korean Strain of Porcine Epidemic Diarrhea Virus

• Published in: Biotechnology and bioprocess engineering Vol. 12; no. 6; pp. 690 - 695
• Main Authors: Park, S.M. (Chonbuk National University, Jeonju, Republic of Korea), Mo, A.Y. (Chonbuk National University, Jeonju, Republic of Korea), Lim, J.G. (Chonbuk National University, Jeonju, Republic of Korea), Chung, H.J. (Chonbuk National University, Jeonju, Republic of Korea), Kim, T.G. (Chonbuk National University, Jeonju, Republic of Korea), Kim, K.J. (Wonkwang University, Iksan, Republic of Korea), Cho, D.H. (Kangwon National University, Chuncheon, Republic of Korea), Yang, M.S. (Chonbuk National University, Jeonju, Republic of Korea), Kim, D.H. (Chonbuk National University, Jeonju, Republic of Korea), E-mail: dhkim@chonbuk.ac.kr
• Format: Journal Article
• Language: English
• Published: Korea (South) Springer Nature B.V 01.12.2007; Springer-Verlag; 한국생물공학회
• Subjects: Amino acids; Antibodies; Bacteria; Epidemics; Feeds; Immune response; Oryza sativa; Porcine epidemic diarrhea virus; Proteins; SACCHAROMYCES CEREVISIAE; surface display; Yeast; Yeasts; 생물공학; surface display; porcine epidemic diarrhea virus; Saccharomyces cerevisiae
• ISSN: 1226-8372; 1976-3816
• DOI: 10.1007/BF02931087

The neutralizing epitope (K-COE) of the spike protein from a Korean strain of porcine epidemic diarrhea virus (PEDV) has been shown to prevent and foster an immune response to PED, when orally adjusted. The cell surface of the budding yeast, Saccharomyces cerevisiae, was engineered to anchor the K-COE on the outer layer of the cell, and consequently, the altered yeast was applied as a dietary complement for animal feed, with immunogenic functions. In this study, the K-COE gene (K-COE) of the Korean strain of PEDV with the signal peptide of rice amylase 1A (Ramy1A), was fused with the gene encoding the carboxyterminal half (320 amino acid residues from the C terminus) of yeast α-agglutinin, a mating associated protein that is anchored covalently to the cell wall.