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

Autor: Yeou-Liang Lin, Jeng-Hwan Wang, Ming-Hwa Jong, Martin Sieber, Jeng-Jer Shieh, Jei-Ming Peng, Shu-Mei Liang, Chi-Ming Liang
Rok vydání: 2003
Předmět:
Protein Folding
Hot Temperature
Swine
T-Lymphocytes
viruses
Dimer
Molecular Sequence Data
Biophysics
Antibodies
Viral
Biophysical Phenomena
Virus
law.invention
chemistry.chemical_compound
Neutralization Tests
law
Escherichia coli
Vaccines
DNA
Animals
Amino Acid Sequence
Polyacrylamide gel electrophoresis
Swine Diseases
Vaccines
Synthetic
General Veterinary
General Immunology and Microbiology
biology
Public Health
Environmental and Occupational Health
Viral Vaccines
biochemical phenomena
metabolism
and nutrition
biology.organism_classification
Molecular biology
Infectious Diseases
Biochemistry
Capsid
chemistry
Foot-and-Mouth Disease Virus
Foot-and-Mouth Disease
Recombinant DNA
biology.protein
Molecular Medicine
Electrophoresis
Polyacrylamide Gel
Immunization
Foot-and-mouth disease virus
Antibody
Cell Division
Cysteine
Zdroj: Vaccine. 21:3721-3729
ISSN: 0264-410X
DOI: 10.1016/s0264-410x(03)00363-3
Popis: 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.
Databáze: OpenAIRE
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