Expression of Human papillomavirus 16 E7ggg oncoprotein on N- and C-terminus of Potato virus X coat protein in bacterial and plant cells

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F11%3A00364095" target="_blank" >RIV/61389030:_____/11:00364095 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.pep.2011.01.008" target="_blank" >http://dx.doi.org/10.1016/j.pep.2011.01.008</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.pep.2011.01.008" target="_blank" >10.1016/j.pep.2011.01.008</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Expression of Human papillomavirus 16 E7ggg oncoprotein on N- and C-terminus of Potato virus X coat protein in bacterial and plant cells

Popis výsledku v původním jazyce

The E7 oncoprotein from Human papillomavirus type 16 (HPV16) is an attractive candidate for anti-cancer therapeutical vaccine development. In this study, we engineered different fusions of mutagenized coding sequence of E7 oncoprotein (E7ggg) with coat protein of Potato virus X (PVX CP) both on 5`- and 3`-terminus of PVX CP and evaluated the influence of the length of linker (no linker, 4, 15 aa) connecting PVX CP and E7ggg on their production. At first the expression in Escherichia coil was conducted to assess the characteristics of the recombinant protein prior to be further produced in plants, that is, resultant proteins were used for screening of their immunological reactivity with antibodies against PVX CP and E7. Fusion proteins successfully expressed in bacteria and plants were partially purified and their reactivity and ability to form virus-like particles were evaluated with anti-E7 antibodies.

Název v anglickém jazyce

Expression of Human papillomavirus 16 E7ggg oncoprotein on N- and C-terminus of Potato virus X coat protein in bacterial and plant cells

Popis výsledku anglicky

The E7 oncoprotein from Human papillomavirus type 16 (HPV16) is an attractive candidate for anti-cancer therapeutical vaccine development. In this study, we engineered different fusions of mutagenized coding sequence of E7 oncoprotein (E7ggg) with coat protein of Potato virus X (PVX CP) both on 5`- and 3`-terminus of PVX CP and evaluated the influence of the length of linker (no linker, 4, 15 aa) connecting PVX CP and E7ggg on their production. At first the expression in Escherichia coil was conducted to assess the characteristics of the recombinant protein prior to be further produced in plants, that is, resultant proteins were used for screening of their immunological reactivity with antibodies against PVX CP and E7. Fusion proteins successfully expressed in bacteria and plants were partially purified and their reactivity and ability to form virus-like particles were evaluated with anti-E7 antibodies.

Druh

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

CEP obor

EI - Biotechnologie a bionika

OECD FORD obor

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Projekt

<a href="/cs/project/GA521%2F09%2F1525" target="_blank" >GA521/09/1525: Biologicky bezpečný expresní systém založený na rostlinných virech pro transientní expresi papillomavirových onkoproteinů a vývoj terapeutické vakcíny</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Protein Expression and Purification

ISSN

1046-5928

e-ISSN

—

Svazek periodika

77

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

146-152

Kód UT WoS článku

000288591900003

EID výsledku v databázi Scopus

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