| Autor: |
Cerovská N; Institute of Experimental Botany v.v.i., Academy of Sciences of the Czech Republic, Na Karlovce 1a, CZ-160 00 Prague 6, Czech Republic. cerovska@ueb.cas.cz, Hoffmeisterová H, Pecenková T, Moravec T, Synková H, Plchová H, Velemínský J |
| Jazyk: |
angličtina |
| Zdroj: |
Protein expression and purification [Protein Expr Purif] 2008 Mar; Vol. 58 (1), pp. 154-61. Date of Electronic Publication: 2007 Sep 18. |
| DOI: |
10.1016/j.pep.2007.09.006 |
| Abstrakt: |
The optimized expression of recombinant Potato virus A coat protein (ACP) carrying two different epitopes from Human papillomavirus type 16 (HPV16) was developed. Epitope derived from minor capsid protein L2 was expressed as N-terminal fusion with ACP while an epitope derived from E7 oncoprotein was fused to its C-terminus. The construct was cloned into Potato X potexvirus (PVX) based vector and transiently expressed in plants using Agrobacterium tumefaciens mediated inoculation. To increase the level of expressed protein the transgenic Nicotiana benthamiana plants expressing Potato virus A HC-Pro gene and transgenic Nicotiana tabacum, cv. Petit Havana SR1 carrying Potato virus A P3 protein gene were tested. Synergistic infection of host plants with PVX carrying the construct and Potato virus Y(O) (PVY(O)) increased the expression of L2ACPE7 in N. tabacum and in transgenic N. benthamiana carrying potyviral HC-Pro gene as compared to control plants infected with L2ACPE7 only. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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