Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 77, Issue 2, Pages 146-152Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2011.01.008
Keywords
Bacterial expression; Human papillomavirus; Oncoprotein E7
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Funding
- Grant Agency of the Czech Republic [521/09/1525]
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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 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. (c) 2011 Elsevier Inc. All rights reserved.
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