Abstract
Potato virus Y(PVY)belongs to the genus Potyvirus.The multifunctional protein coat protein(CP)of PVY is involved in the virus genome replication,aphid transmission,cell-to-cell and long-distance move-ment,symptom formation,etc.Our previous results have revealed that multiple sites within CP are potentially acetylated.However,the effect of acetylation on those potential sites of CP on PVY infection is still unclear.In this study,we mutated the identified sites,K12,K13,K16,K28 and K32 located at the N terminal,K177,K221 and K226 located at the central domain and K265 located at the C-terminal,to acetylation mimicking residue glutamine and non-acetylation residue arginine,respectively.We analyzed the infectivity of 18 PVY mutants on Nicotiana tabacum cv Xanthi plants.It showed that most of the mutants containing a single mutation have no apparent effect on the pathogenicity of PVY on N.tabacum cv Xanthi.Non-acetylation mutation at sites K16and K265 abol-ished the ability of PVY to induce vein necrosis.Both non-acetylation and acetylation at site K221 reduced PVY replication,and these modifications also abolished the ability of PVY mutants to move between cells.This is the first report to reveal the effect of potential acetylation in CP on PVY infection.These results will enhance our un-derstanding of the role of post-translational modification during PVY infection.
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