title: A short motif in the N-terminal part of the coat protein is a host-specific determinant of systemic infectivity for two potyviruses.
abstract: Although the biological variability of Watermelon mosaic virus is limited, isolates from the three main molecular groups differ in their ability to infect systemically Chenopodium 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 (Lys-Glu-Ala) or KEA, systemic on C. quinoa), group 2 (Lys-Glu-Thr 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.
authors.affiliation: UR0407 Pathologie Végétale, INRA, F-84140, Montfavet, France.
authors.forename: Cecile
authors.initials: C
authors.lastname: Desbiez
authors.forename: Charlotte
authors.initials: C
authors.lastname: Chandeysson
authors.forename: Herve
authors.initials: H
authors.lastname: Lecoq
mesh_terms: D036022:Capsid Proteins / Q000737:chemistry / Q000502:physiology*; D027465:Chenopodium quinoa / Q000821:virology*; D017800:Potyvirus / Q000378:metabolism / Q000472:pathogenicity*; D014774:Virulence
chemical_list: D036022:Capsid Proteins