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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10294229" target="_blank" >RIV/00216208:11310/15:10294229 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61389030:_____/15:00446182 RIV/00023736:_____/15:00011089

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s11240-014-0634-x" target="_blank" >http://dx.doi.org/10.1007/s11240-014-0634-x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11240-014-0634-x" target="_blank" >10.1007/s11240-014-0634-x</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

—

Projekt

<a href="/cs/project/GAP501%2F12%2F1761" target="_blank" >GAP501/12/1761: Vliv topologie heterologních antigenních determinant ve vektoru odvozeném od X viru bramboru (PVX) na jejich expresi v rostlinách a imunogenitu</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Plant Cell, Tissue and Organ Culture

ISSN

0167-6857

e-ISSN

—

Svazek periodika

120

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

10

Strana od-do

671-680

Kód UT WoS článku

000348807200022

EID výsledku v databázi Scopus

2-s2.0-84925520137