Open AccessA short motif in the N ‐terminal part of the coat protein is a host‐specific determinant of systemic infectivity for two potyviruses
Author(s) -
Desbiez Cecile,
Chandeysson Charlotte,
Lecoq Herve
Publication year - 2014
Publication title -
molecular plant pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.945
H-Index - 103
eISSN - 1364-3703
pISSN - 1464-6722
DOI - 10.1111/mpp.12076
Subject(s) - biology , chenopodium quinoa , infectivity , virus , virology , amino acid , coat protein , genetics , botany , gene , rna
Summary Although the biological variability of Watermelon mosaic virus is limited, isolates from the three main molecular groups differ in their ability to infect systemically C henopodium quinoa . Mutations were introduced in a motif of three or five amino acids located in the N ‐terminal part of the coat protein, and differing in isolates from group 1 (motif: lysine‐glutamic acid‐alanine ( L ys‐ G lu‐ A la) or KEA , systemic on C . quinoa ), group 2 ( L ys‐ G lu‐ T hr or KET , not systemic on C . quinoa ) and group 3 ( KEKET , not systemic on C . quinoa ). Mutagenesis of KEKET in an isolate from group 3 to KEA or KEKEA was sufficient to make the virus systemic on C . quinoa , whereas mutagenesis to KET had no effect. Introduction of a KEA motif in Zucchini yellow mosaic virus coat protein also resulted in systemic infection on C . quinoa . These mutations had no obvious effect on the disorder profile or potential post‐translational modifications of the coat protein as determined in silico .