New positions for peptide presentation in Potato virus X capsid protein

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10296477" target="_blank" >RIV/00216208:11310/15:10296477 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61389030:_____/15:00446883

Výsledek na webu

<a href="http://dx.doi.org/10.1515/biol-2015-0019" target="_blank" >http://dx.doi.org/10.1515/biol-2015-0019</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1515/biol-2015-0019" target="_blank" >10.1515/biol-2015-0019</a>

Jazyk výsledku

angličtina

Název v původním jazyce

New positions for peptide presentation in Potato virus X capsid protein

Popis výsledku v původním jazyce

Potato virus X (PVX) is widely used as a peptide presentation system in plant biotechnology, mostly for transient expression of desired peptides fused to the N-terminus of its capsid protein (CP). Here we describe testing/investigation of new positions for peptide presentation based on seven putative surface loops of PVX CP. We performed bacterial expression of fourteen different PVX CPs modified by the insertion of the epitope derived from the E7 oncoprotein (E7 epitope) of Human papillomavirus type 16fused with His tag. The expression from vector pMPM-A4O in Escherichia coli MC1061 was performed to evaluate the capacity of the PVX CP platform to tolerate the insertion of E7 epitope fused with His tag in the seven putative surface loops. The immunological characteristics of expressed epitopes were assessed by Western blot using both anti-PVX CP and anti-His antibodies and by immunoelectron microscopy.

Název v anglickém jazyce

New positions for peptide presentation in Potato virus X capsid protein

Popis výsledku anglicky

Potato virus X (PVX) is widely used as a peptide presentation system in plant biotechnology, mostly for transient expression of desired peptides fused to the N-terminus of its capsid protein (CP). Here we describe testing/investigation of new positions for peptide presentation based on seven putative surface loops of PVX CP. We performed bacterial expression of fourteen different PVX CPs modified by the insertion of the epitope derived from the E7 oncoprotein (E7 epitope) of Human papillomavirus type 16fused with His tag. The expression from vector pMPM-A4O in Escherichia coli MC1061 was performed to evaluate the capacity of the PVX CP platform to tolerate the insertion of E7 epitope fused with His tag in the seven putative surface loops. The immunological characteristics of expressed epitopes were assessed by Western blot using both anti-PVX CP and anti-His antibodies and by immunoelectron microscopy.

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

Open Life Sciences [online]

ISSN

2391-5412

e-ISSN

—

Svazek periodika

10

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

PL - Polská republika

Počet stran výsledku

9

Strana od-do

133-141

Kód UT WoS článku

000354077300015

EID výsledku v databázi Scopus

2-s2.0-84927920126