Induction of immunity in swine by purified recombinant VP1 of foot-and-mouth disease virus

• Published in: Vaccine Vol. 21; no. 25-26; pp. 3721 - 3729
• Main Authors: Wang, Jeng-Hwan, Liang, Chi-Ming, Peng, Jei-Ming, Shieh, Jeng-Jer, Jong, Ming-Hwa, Lin, Yeou-Liang, Sieber, Martin, Liang, Shu-Mei
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Ltd 08.09.2003; Elsevier Limited
• Subjects: Amino Acid Sequence; Amino acids; Animals; Antibodies; Antibodies, Viral - biosynthesis; Antibodies, Viral - genetics; Binding sites; Biophysical Phenomena; Biophysics; Capsid protein; Cell Division - physiology; Chemical bonds; Cloning; Dimerization; Dimers; E coli; Electrophoresis, Polyacrylamide Gel; Epitopes; Escherichia coli - metabolism; FMDV; Foot & mouth disease; Foot-and-Mouth Disease - prevention & control; Foot-and-mouth disease virus; Foot-and-Mouth Disease Virus - immunology; Heat treatment; Hot Temperature; Immune response; Immunity; Immunity (Disease); Immunization; Immunoglobulins; Lymphocytes; Molecular Sequence Data; Monomers; Neutralization Tests; Peptides; Protein Folding; Proteins; Recombinant protein; Refolding; Swine; Swine - immunology; Swine Diseases - prevention & control; T-Lymphocytes - immunology; Vaccination; Vaccines; Vaccines, DNA - immunology; Vaccines, Synthetic - immunology; Viral Vaccines - biosynthesis; Viral Vaccines - genetics; Viral Vaccines - immunology; Viruses; VP1 protein; Taiwan; FMDV; Refolding; Recombinant protein
• ISSN: 0264-410X; 1873-2518
• DOI: 10.1016/S0264-410X(03)00363-3

VP1, a capsid protein of foot-and-mouth disease virus (FMDV), contains neutralizing epitopes of the virus. Due to its poor water solubility, recombinant Escherichia coli derived VP1 (rVP1) has previously been used mainly in a denatured form and is not well characterized. Here, using SDS to assist protein refolding and then removing SDS with a detergent removing column, we have successfully purified rVP1 in two aqueous-soluble forms, i.e. monomer and dimer. Studies showed that dimerization occurs by an inter-molecular disulfide bond between two cysteine residues at position 187 of each monomer. Heat treatment revealed that rVP1 dimer exhibited a more thermal-stable conformation than the monomeric form. Both monomeric and dimeric rVP1 reacted with anti-FMDV antibodies. Immunization studies demonstrated that vaccination of swine with either forms of rVP1 was effective in generating immune responses and protecting them from viral challenge.