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Potato virus X displaying the E7 peptide derived from human papillomavirus type 16: a novel position for epitope presentation

  1. 1.
    0446182 - ÚEB 2016 RIV NL eng J - Článek v odborném periodiku
    Vaculík, Petr - Plchová, Helena - Moravec, Tomáš - Hoffmeisterová, Hana - Čeřovská, Noemi - Šmahel, M.
    Potato virus X displaying the E7 peptide derived from human papillomavirus type 16: a novel position for epitope presentation.
    Plant Cell, Tissue and Organ Culture. Roč. 120, č. 2 (2015), s. 671-680. ISSN 0167-6857. E-ISSN 1573-5044
    Grant CEP: GA ČR(CZ) GAP501/12/1761
    Grant ostatní: European Regional Development Fund(XE) CZ.2.16/3.1.00/24014
    Institucionální podpora: RVO:61389030
    Klíčová slova: Potato virus X * Human papillomavirus * Nicotiana benthamiana
    Kód oboru RIV: EE - Mikrobiologie, virologie
    Impakt faktor: 2.390, rok: 2015

    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.
    Trvalý link: http://hdl.handle.net/11104/0248166

     
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