Analysis of potyvirus terminal protein VPg-transgenic Arabidopsis thaliana plants.

Izabela Wojtal; Paulina Piontek; Renata Grzela; Artur Jarmołowski; Włodzimierz Zagórski; Jadwiga Chroboczek

doi:10.18388/abp.2011_2245

Analysis of potyvirus terminal protein VPg-transgenic Arabidopsis thaliana plants.

Izabela Wojtal Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland.;
Paulina Piontek
Renata Grzela
Artur Jarmołowski
Włodzimierz Zagórski
Jadwiga Chroboczek

DOI: https://doi.org/10.18388/abp.2011_2245

Abstract

Virus-coded VPg protein of Potato virus Y (PVY) does not have homologs apart from other VPgs. Since VPg is indispensable for the potyvirus life cycle, it appeared a good candidate for eliciting pathogen-derived resistance to PVY. Following agroinfection used to obtain PVY VPg-transgenic Arabidopsis thaliana plants, only few transgenic seeds were recovered giving rise to six transgenic plants that contained the VPg gene with the correct sequence. They generated VPg mRNA, but VPg protein was not detected. Some plants were immune to PVY infection suggesting post-transcriptional gene silencing. However, the likely PVY VPg toxicity exerted at an early stage of transformed seeds development precludes its use for engineering pathogen-derived resistance.

Published

2011-09-13

Issue

Vol. 58 No. 3 (2011)

Section

Articles

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