Abstract
A codon optimized DNA sequence coding for foot-and-mouth disease virus (FMDV) capsid protein complex epitopes of VP1 amino acid residues 21-40, 135-160, and 200-213 was genetically fused to the C-terminal end of a glutathione-S-transferase (GST) gene in pGEX-6P-1 vector with the synonymous codons preferred by Escherichia coli . The gene was synthesized using PCR and subsequently expressed in E. coli producing an intracellular, soluble fusion protein that retained antigenicity associated with FMDV antibodies by western blot analysis. The chimera was purified from bacterial lysates by affinity chromatography and could be used in ELISA tests for antibodies against FMDV.
Publication types
-
Evaluation Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Antibodies / analysis*
-
Antibodies / immunology
-
Capsid Proteins / biosynthesis*
-
Capsid Proteins / genetics
-
Capsid Proteins / immunology
-
Cattle
-
Codon / genetics
-
Enzyme-Linked Immunosorbent Assay / methods*
-
Epitopes / genetics
-
Epitopes / immunology
-
Epitopes / metabolism*
-
Escherichia coli / genetics
-
Escherichia coli / metabolism*
-
Foot-and-Mouth Disease / blood
-
Foot-and-Mouth Disease / virology
-
Foot-and-Mouth Disease Virus / immunology
-
Foot-and-Mouth Disease Virus / metabolism*
-
Protein Engineering / methods*
-
Recombinant Fusion Proteins / immunology
-
Recombinant Fusion Proteins / metabolism
-
Sheep
-
Swine
Substances
-
Antibodies
-
Capsid Proteins
-
Codon
-
Epitopes
-
Recombinant Fusion Proteins