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Detection of foot-and-mouth virus antibodies using a purified protein from the high-level expression of codon-optimized, foot-and-mouth disease virus complex epitopes in Escherichia coli.

Authors
  • Song, Houhui
  • Fang, Weihuan
  • Wang, Zhiliang
  • Zheng, Dongxia
  • Du, Jian
  • Li, Hong
  • Li, Yong
  • Qiu, Bingsheng
Type
Published Article
Journal
Biotechnology letters
Publication Date
Aug 01, 2004
Volume
26
Issue
16
Pages
1277–1281
Identifiers
PMID: 15483387
Source
Medline
License
Unknown

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.

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