High-yield production of the VP1 structural protein epitope from serotype O foot-and-mouth disease virus in Escherichia coli

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For effective control of foot-and-mouth disease (FMD), the development of rapid diagnostic systems and vaccines are required against its etiological agent, FMD virus (FMDV). To accomplish this, efficient large-scale expression of the FMDV VP1 protein, with high solubility, needs to be optimized. We attempted to produce high levels of a serotype O FMDV VP1 epitope in Escherichia coli. We identified the subtype-independent serotype O FMDV VP1 epitope sequence and used it to construct a glutathione S-transferase (GST) fusion protein. For efficient production of the FMDV VP1 epitope fused to GST (VP1e-GST), four E. coli strains and three temperatures were examined. The conditions yielding the greatest level of VP1e-GST with highest solubility were achieved with E. coli BL21(DE3) at 25 A degrees C. For high-level production, fed-batch cultures were conducted in 5-l bioreactors. When cells were induced at a high density and complex feeding solutions were supplied, approximately 11 g of VP1e-GST was obtained from a 2.9-l culture. Following purification, the VP1 epitope was used to immunize rabbits, and we confirmed that it induced an immune response.
Publisher
SPRINGER HEIDELBERG
Issue Date
2013-07
Language
English
Article Type
Article
Keywords

G-H LOOP; HIGH-LEVEL PRODUCTION; HUMAN LEPTIN; EXPRESSION; BATCH; CULTIVATION; CULTURE; ANTIGEN; SWINE

Citation

JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY, v.40, no.7, pp.705 - 713

ISSN
1367-5435
DOI
10.1007/s10295-013-1273-7
URI
http://hdl.handle.net/10203/175031
Appears in Collection
CBE-Journal Papers(저널논문)
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