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

0364095 - ÚEB 2012 RIV US eng J - Journal Article
Plchová, Helena - Moravec, Tomáš - Hoffmeisterová, Hana - Folwarczna, Jitka - Čeřovská, Noemi
Expression of Human papillomavirus 16 E7ggg oncoprotein on N- and C-terminus of Potato virus X coat protein in bacterial and plant cells.
Protein Expression and Purification. Roč. 77, č. 2 (2011), s. 146-152. ISSN 1046-5928. E-ISSN 1096-0279
R&D Projects: GA ČR GA521/09/1525
Institutional research plan: CEZ:AV0Z50380511
Keywords : Bacterial expression * Human papillomavirus * Oncoprotein E7
Subject RIV: EI - Biotechnology ; Bionics
Impact factor: 1.587, year: 2011

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.
Permanent Link: http://hdl.handle.net/11104/0199666