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Point mutations in helper component protease of clover yellow vein virus are associated with the attenuation of RNA-silencing suppression activity and symptom expression in broad bean

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Title: Point mutations in helper component protease of clover yellow vein virus are associated with the attenuation of RNA-silencing suppression activity and symptom expression in broad bean
Authors: Yambao, M. L. M. Browse this author
Yagihashi, H. Browse this author
Sekiguchi, H. Browse this author
Sekiguchi, T. Browse this author
Sasaki, T. Browse this author
Sato, M. Browse this author
Atsumi, G. Browse this author
Tacahashi, Y. Browse this author
Nakahara, K. S. Browse this author →KAKEN DB
Uyeda, I. Browse this author →KAKEN DB
Issue Date: Jan-2008
Publisher: Springer Wien
Journal Title: Archives of Virology
Volume: 153
Issue: 1
Start Page: 105
End Page: 115
Publisher DOI: 10.1007/s00705-007-1073-3
PMID: 17955160
Abstract: Helper component protease (HC-Pro) is a potyvirus-encoded multifunctional protein and a major determinant of symptom expression in a susceptible plant. Here, we show the involvement of clover yellow vein virus (ClYVV) HC-Pro in necrotic symptom expression in broad bean (Vicia faba cv. Wase). In this host, lethal necrosis was induced by ClYVV no. 30, from which a spontaneous, mosaic-inducing mutant (MM) was obtained. Mapping with chimeric viruses between ClYVV no. 30 and MM attributed the symptom attenuation to two mutations at the HC-Pro positions 27 (threonine to isoleucine) and 193 (aspartic acid to tyrosine). Although neither mutant with the single amino acid substitution at position 27 or 193 (ClYVV/T27I or D193Y) induced the lethal necrosis, ClYVV/T27I still retained the ability to induce necrotic symptoms, but ClYVV/D193Y scarcely did so. The virus accumulation of ClYVV/D193Y was also lower than that of ClYVV no. 30. The mutations, T27I and D193Y, are located in a putative zinc finger domain and in one (N-terminal) of the two RNA binding domains, respectively, of HC-Pro. RNA-silencing suppression (RSS) activity of P1/HC-Pro in Nicotiana benthamiana was weakened by both mutations. Our results suggest a correlation between viral virulence and RSS function and the importance of the two domains in HC-Pro.
Rights: The original publication is available at www.springerlink.com
Relation: http://www.springerlink.com
Type: article (author version)
URI: http://hdl.handle.net/2115/33039
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 中原 健二

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