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: Cecile Desbiez, Charlotte Chandeysson, Herve Lecoq
• Journal: Molecular plant pathology (Mol Plant Pathol) Vol. 15 Issue 2 Pg. 217-21 (Feb 2014) ISSN: 1364-3703 [Electronic] England
• PMID: 24118745 (Publication Type: Journal Article)
• Copyright: © 2013 BSPP AND JOHN WILEY & SONS LTD.

Chemical References

• Capsid Proteins

Topics

• Capsid Proteins (chemistry, physiology)
• Chenopodium quinoa (virology)
• Potyvirus (metabolism, pathogenicity)
• Virulence