Počet záznamů: 1
Heterologous expression of full-length capsid protein of porcine circovirus 2 in Escherichia coli and its potential use for detection of antibodies
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SYSNO ASEP 0334821 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Heterologous expression of full-length capsid protein of porcine circovirus 2 in Escherichia coli and its potential use for detection of antibodies Tvůrce(i) 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, ORCIDZdroj.dok. Journal of Virological Methods. - : Elsevier - ISSN 0166-0934
Roč. 162, 1-2 (2009), s. 133-141Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. NL - Nizozemsko Klíč. slova PCV 2 ; Porcine circovirus ; Capsid protein Vědní obor RIV EE - Mikrobiologie, virologie CEP GP310/07/P115 GA ČR - Grantová agentura ČR 2B06161 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000271586500020 DOI 10.1016/j.jviromet.2009.07.028 Anotace 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 Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2010
Počet záznamů: 1