Expression of Human papillomavirus 16 E7ggg oncoprotein on N- and C-terminus of Potato virus X coat protein in bacterial and plant cells
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
21266198
DOI
10.1016/j.pep.2011.01.008
PII: S1046-5928(11)00019-2
Knihovny.cz E-resources
- MeSH
- 3' Flanking Region MeSH
- 5' Flanking Region MeSH
- Agrobacterium tumefaciens MeSH
- Escherichia coli MeSH
- Gene Expression MeSH
- Papillomavirus Infections immunology virology MeSH
- Cloning, Molecular MeSH
- Humans MeSH
- Human papillomavirus 16 genetics immunology metabolism MeSH
- Uterine Cervical Neoplasms immunology virology MeSH
- Papillomavirus E7 Proteins genetics immunology metabolism MeSH
- Potexvirus genetics immunology metabolism MeSH
- Protein Engineering methods MeSH
- Antibodies immunology MeSH
- Recombinant Fusion Proteins genetics immunology metabolism MeSH
- Nicotiana MeSH
- Papillomavirus Vaccines chemistry genetics MeSH
- Capsid Proteins genetics immunology metabolism MeSH
- Vaccines, Virus-Like Particle chemistry genetics MeSH
- Check Tag
- Humans MeSH
- Female MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- coat protein, Potato virus X MeSH Browser
- Papillomavirus E7 Proteins MeSH
- Antibodies MeSH
- Recombinant Fusion Proteins MeSH
- Papillomavirus Vaccines MeSH
- Capsid Proteins MeSH
- Vaccines, Virus-Like Particle MeSH
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, 15aa) connecting PVX CP and E7ggg on their production. At first the expression in Escherichia coli 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.
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