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Oral immunization against foot-and-mouth disease virus using recombinant Saccharomyces cerevisiae with the improved expression of the codon-optimized VP1 fusion protein.
Le, Ngoc My Tieu; So, Kum-Kang; Kim, Dae-Hyuk.
Afiliación
  • Le NMT; Department of Bioactive Material Sciences, Jeonbuk National University, Jeonju, Jeonbuk 54896, Republic of Korea.
  • So KK; Institute for Molecular Biology and Genetics, Jeonbuk National University, Jeonju, Jeonbuk, 54896 Republic of Korea.
  • Kim DH; Department of Bioactive Material Sciences, Jeonbuk National University, Jeonju, Jeonbuk 54896, Republic of Korea; Institute for Molecular Biology and Genetics, Jeonbuk National University, Jeonju, Jeonbuk, 54896 Republic of Korea; Department of Molecular Biology, Jeonbuk National University, Jeonju, Jeonbuk 54896, Republic of Korea. Electronic address: dhkim@jbnu.ac.kr.
Vet Microbiol ; 296: 110192, 2024 Sep.
Article en En | MEDLINE | ID: mdl-39032444
ABSTRACT
VP1, a major immunogenic protein of foot-and-mouth disease virus (FMDV), facilitates viral attachment and entry into host cells. VP1 possesses critical epitope sequences responsible for inducing neutralizing antibodies but its expression using Saccharomyces cerevisiae has been hampered despite evidence that the presence of VP1 does not negatively impact the yeast's biology. In this study, we fused proteins to enhance VP1 expression using S. cerevisiae. Among short P1 chimeras containing VP1 including VP3-VP1 and VP2-VP1, VP3-VP1 fusion proteins showed higher expression levels than VP2-VP1. We subsequently designed new fusion proteins, of which 20 amino acids of N-terminal VP3 fused with VP1-Co1 (referred to 20aaVP3-VP1-Co1) showed the highest expression level. Lowering the culture temperature from 30 °C to 20 °C further enhanced fusion protein production. The highest expression level of 20aaVP3-VP1-Co1 was estimated to be 7.7 mg/L, which is comparable to other heterologous proteins produced using our S. cerevisiae expression system. Oral administration of the cell expressing 20aaVP3-VP1-Co1 induced VP1-specific IgG and IgA responses in mice. The S. cerevisiae-expressed 20aaVP3-VP1-Co1 fusion protein induced a significant immune response to the FMDV structural epitope protein, which opens the possibility of an oral FMDV vaccine.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteínas Recombinantes de Fusión / Vacunas Virales / Virus de la Fiebre Aftosa / Proteínas de la Cápside / Fiebre Aftosa / Anticuerpos Antivirales Límite: Animals Idioma: En Revista: Vet Microbiol Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteínas Recombinantes de Fusión / Vacunas Virales / Virus de la Fiebre Aftosa / Proteínas de la Cápside / Fiebre Aftosa / Anticuerpos Antivirales Límite: Animals Idioma: En Revista: Vet Microbiol Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos