Sarasate EiamtanasateMila JuricekYun Kiam YapMahidol UniversityInstitute of Experimental Botany of the Academy of Sciences of the Czech Republic2018-08-242018-08-242007-12-01Virus Genes. Vol.35, No.3 (2007), 611-6171572994X092085692-s2.0-35549004578https://repository.li.mahidol.ac.th/handle/20.500.14594/24072P3 protein is one of the least characterized potyviral proteins in both functions and sub-cellular localization. In this study, we examined the sub-cellular localization of PRSV P3 and its intermediate, P3-6K1by expressing their GFP fusion proteins in onion epidermal cells. Our results showed that both P3- and P3-6K1GFP fusion proteins were localized at the endoplasmic reticulum. Deletion analysis indicated that C-terminal of P3 protein contained localization signal, and a 19 amino acids hydrophobic domain from this region was able to target the GFP fusion protein to endoplasmic reticulum. C-terminal of P3 proteins has been suggested to be involved in both viability and pathogenicity of the potyvirus. Therefore, our result suggests that localization of P3 protein at endoplasmic reticulum is essential for functionality of P3 protein. © 2007 Springer Science+Business Media, LLC.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyImmunology and MicrobiologyC-terminal hydrophobic region leads PRSV P3 protein to endoplasmic reticulumArticleSCOPUS10.1007/s11262-007-0114-z