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Efficient expression of Human papillomavirus 16 E7 oncoprotein fused to C-terminus of Tobacco mosaic virus (TMV) coat protein using molecular chaperones in Escherichia coli

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10125286" target="_blank" >RIV/00216208:11310/12:10125286 - isvavai.cz</a>

  • Alternative codes found

    RIV/61389030:_____/12:00380787

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.pep.2012.07.008" target="_blank" >http://dx.doi.org/10.1016/j.pep.2012.07.008</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.pep.2012.07.008" target="_blank" >10.1016/j.pep.2012.07.008</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Efficient expression of Human papillomavirus 16 E7 oncoprotein fused to C-terminus of Tobacco mosaic virus (TMV) coat protein using molecular chaperones in Escherichia coli

  • Original language description

    The Human papillomavirus 16 (HPV16)E7 oncoprotein is a promising candidate for development of anticancer therapeutic vaccine. We have prepared the expression construct carrying mutagenized E7 oncoprotein fused to the C-terminus of Tobacco mosaic virus (TMV) coat protein via 15 amino acids beta-sheet linker. The fusion protein was expressed in Escherichia coli MC 1061 cells. We have obtained high level expression, but most of the protein remained in insoluble inclusion bodies. To increase the ratio of soluble protein various molecular chaperones (TF, DnaK-Dnai-GrpE, GroEL-GroES) were used. The immunological reactivity of expressed recombinant protein was evaluated with anti-E7 and anti-TMV antibodies. The distribution of expressed product during ultracentrifugation on sucrose gradient was studied. (c) 2012 Elsevier Inc. All rights reserved.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EI - Biotechnology and bionics

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2012

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Protein Expression and Purification

  • ISSN

    1046-5928

  • e-ISSN

  • Volume of the periodical

    85

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    6

  • Pages from-to

    152-157

  • UT code for WoS article

    000308630400021

  • EID of the result in the Scopus database