Čeština
EnglishExpression of Human papillomavirus 16 E7ggg oncoprotein on N- and C- terminus of Potato virus X coat protein in bacterial and plant cells
Plchova H., Moravec T., Hoffmeisterova H., Folwarczna J., Cerovska N.
PROTEIN EXPRESSION AND PURIFICATION 77: 146-152, 2011
Keywords: Bacterial expression, Human papillomavirus, Oncoprotein E7
Abstract: 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.
DOI:
Fulltext: contact IEB authors
IEB authors: Noemi Čeřovská, Hana Hoffmeisterová, Tomáš Moravec, Helena Plchová
PROTEIN EXPRESSION AND PURIFICATION 77: 146-152, 2011
Keywords: Bacterial expression, Human papillomavirus, Oncoprotein E7
Abstract: 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.
DOI:
Fulltext: contact IEB authors
IEB authors: Noemi Čeřovská, Hana Hoffmeisterová, Tomáš Moravec, Helena Plchová