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Heterologous expression of full-length capsid protein of porcine circovirus 2 in Escherichia coli and its potential use for detection of antibodies

SYSNO ASEP	0334821
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Heterologous expression of full-length capsid protein of porcine circovirus 2 in Escherichia coli and its potential use for detection of antibodies
Author(s)	Marčeková, Zuzana (MBU-M) Psikal, P. (CZ) Kosinová, E. (CZ) Benada, Oldřich (MBU-M)_{ORCID, RID} Šebo, Peter (MBU-M)_{RID, ORCID} Bumba, Ladislav (MBU-M)_{RID, ORCID}
Source Title	Journal of Virological Methods. - : Elsevier - ISSN 0166-0934 Roč. 162, 1-2 (2009), s. 133-141
Number of pages	9 s.
Language	eng - English
Country	NL - Netherlands
Keywords	PCV 2 ; Porcine circovirus ; Capsid protein
Subject RIV	EE - Microbiology, Virology
R&D Projects	GP310/07/P115 GA ČR - Czech Science Foundation (CSF)
	2B06161 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
CEZ	AV0Z50200510 - MBU-M (2005-2011)
UT WOS	000271586500020
DOI	10.1016/j.jviromet.2009.07.028
Annotation	A capsid protein of porcine circovirus 2 (PCV 2) serves as a diagnostic antigen for the detection of PCV 2-associated disease known as a postweaning multisystemic wasting syndrome (PMWS). In this report, a bacterial expression system was developed for the expression and purification of the full-length PCV 2 capsid (Cap) protein from a codon-optimized cap gene. Replacement of rare arginine codons located at the 5_ end of the cap reading frame with codons optimal for E. coli was found to overcome the poor expression of the viral protein in the prokaryotic system. The Cap protein was purified to greater than 95% homogeneity by using a single cation-exchange chromatography at a yield of 10mg per litre of bacterial culture
Workplace	Institute of Microbiology
Contact	Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
Year of Publishing	2010

Number of the records: 1