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Potato virus X displaying the E7 peptide derived from human papillomavirus type 16: a novel position for epitope presentation
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SYSNO ASEP 0446182 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Potato virus X displaying the E7 peptide derived from human papillomavirus type 16: a novel position for epitope presentation Author(s) Vaculík, Petr (UEB-Q) RID
Plchová, Helena (UEB-Q) RID, ORCID
Moravec, Tomáš (UEB-Q) RID, ORCID
Hoffmeisterová, Hana (UEB-Q) RID
Čeřovská, Noemi (UEB-Q) RID, ORCID
Šmahel, M. (CZ)Source Title Plant Cell, Tissue and Organ Culture. - : Springer - ISSN 0167-6857
Roč. 120, č. 2 (2015), s. 671-680Number of pages 10 s. Language eng - English Country NL - Netherlands Keywords Potato virus X ; Human papillomavirus ; Nicotiana benthamiana Subject RIV EE - Microbiology, Virology R&D Projects GAP501/12/1761 GA ČR - Czech Science Foundation (CSF) Institutional support UEB-Q - RVO:61389030 UT WOS 000348807200022 DOI 10.1007/s11240-014-0634-x Annotation Potato virus X (PVX) is widely used as a peptide presentation system in plant biotechnology, mostly by fusion of desired peptides to the N-terminus of its capsid protein (CP). Considering that some epitopes can interfere with the stability and/or self-assembly of PVX CP when fused to its N-terminus, we evaluated four other possible sites for fusion using the E7 epitope derived from human papillomavirus type 16 with different tags. We prepared eight different PVX CP constructs modified with the E7 epitope fused with the 6xHis tag in both orientations (6xHis-E7, E7-6xHis), cloned them into the PVX-based vector pGR106 and expressed them transiently in Nicotiana benthamina plants. Only the fusion site located after amino acid 23 led to systemic infection of plants and the production of recombinant proteins, but no viral particles were detected. When we replaced the 6xHis with StrepII tag, the modified virus infected plants systemically, expressed proteins assembled into viral particles and the epitopes were located on the particle surface. The results of this study indicate that the new position within the PVX CP can be used for peptide presentation on the surface of PVX particles and is promising for PVX based production of therapeutic compounds in plants. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2016
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