{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T17:14:12Z","timestamp":1781716452601,"version":"3.54.5"},"reference-count":61,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2013,3,4]],"date-time":"2013-03-04T00:00:00Z","timestamp":1362355200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["bsppjournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Plant Pathology"],"published-print":{"date-parts":[[2013,4]]},"abstract":"Summary<\/jats:title>\n \n Cysteine\u2010rich proteins (\n CRPs<\/jats:styled-content>\n ) encoded by some plant viruses in diverse genera function as\n RNA<\/jats:styled-content>\n silencing suppressors. Within the\n N<\/jats:styled-content>\n \u2010terminal portion of\n CRPs<\/jats:styled-content>\n encoded by furoviruses, there are six conserved cysteine residues and a\n C<\/jats:styled-content>\n ys\u2013\n G<\/jats:styled-content>\n ly\u2013\n X<\/jats:styled-content>\n \u2013\n X<\/jats:styled-content>\n \u2013\n H<\/jats:styled-content>\n is motif (\n C<\/jats:styled-content>\n ys, cysteine;\n G<\/jats:styled-content>\n ly, glycine;\n H<\/jats:styled-content>\n is, histidine;\n X<\/jats:styled-content>\n , any amino acid residue) with unknown function. The central domains contain coiled\u2010coil heptad amino acid repeats that usually mediate protein dimerization. Here, we present evidence that the conserved cysteine residues and\n C<\/jats:styled-content>\n ys\u2013\n G<\/jats:styled-content>\n ly\u2013\n X<\/jats:styled-content>\n \u2013\n X<\/jats:styled-content>\n \u2013\n H<\/jats:styled-content>\n is motif in the\n CRP<\/jats:styled-content>\n of\n \n C<\/jats:styled-content>\n hinese wheat mosaic virus\n <\/jats:italic>\n (\n CWMV<\/jats:styled-content>\n ) are critical for protein stability and silencing suppression activity. Mutation of a leucine residue in the third coiled\u2010coil heptad impaired\n CWMV CRP<\/jats:styled-content>\n activity for suppression of local silencing, but not for the promotion of cell\u2010to\u2010cell movement of\n \n P<\/jats:styled-content>\n otato virus\n X<\/jats:styled-content>\n <\/jats:italic>\n (\n PVX<\/jats:styled-content>\n ).\n In\u2009planta<\/jats:italic>\n and\n in\u2009vitro<\/jats:italic>\n analysis of wild\u2010type and mutant proteins indicated that the ability of the\n CRP<\/jats:styled-content>\n to self\u2010interact was correlated with its suppression activity. Deletion of up to 40 amino acids at the\n C<\/jats:styled-content>\n \u2010terminus did not abolish suppression activity, but disrupted the association of\n CRP<\/jats:styled-content>\n with endoplasmic reticulum (\n ER<\/jats:styled-content>\n ), and reduced its activity in the enhancement of\n PVX<\/jats:styled-content>\n symptom severity. Interestingly, a short region in the\n C<\/jats:styled-content>\n \u2010terminal domain, predicted to form an amphipathic \u03b1\u2010helical structure, was responsible for the association of\n CWMV CRP<\/jats:styled-content>\n with\n ER<\/jats:styled-content>\n . Overall, our results demonstrate that the\n N<\/jats:styled-content>\n \u2010terminal and central regions are the functional domains for suppression activity, whereas the\n C<\/jats:styled-content>\n \u2010terminal region primarily functions to target\n CWMV CRP<\/jats:styled-content>\n to the\n ER<\/jats:styled-content>\n .\n <\/jats:p>","DOI":"10.1111\/mpp.12002","type":"journal-article","created":{"date-parts":[[2013,3,5]],"date-time":"2013-03-05T05:22:54Z","timestamp":1362460974000},"page":"265-278","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":57,"title":["Identification of the amino acid residues and domains in the cysteine\u2010rich protein of\n \n C<\/scp>\n hinese wheat mosaic virus\n <\/i>\n that are important for\n RNA<\/scp>\n silencing suppression and subcellular localization"],"prefix":"10.1111","volume":"14","author":[{"given":"Liying","family":"Sun","sequence":"first","affiliation":[{"name":"State Key Laboratory Breeding Base for Zhejiang Sustainable Pest and Disease Control Ministry of Agriculture Key Laboratory of Biotechnology in Plant Protection Institute of Virology and Biotechnology Zhejiang Academy of Agricultural Sciences Hangzhou 310021 China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ida Bagus","family":"Andika","sequence":"additional","affiliation":[{"name":"State Key Laboratory Breeding Base for Zhejiang Sustainable Pest and Disease Control Ministry of Agriculture Key Laboratory of Biotechnology in Plant Protection Institute of Virology and Biotechnology Zhejiang Academy of Agricultural Sciences Hangzhou 310021 China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hideki","family":"Kondo","sequence":"additional","affiliation":[{"name":"Institute of Plant Science and Resources (IPSR) Okayama University Kurashiki 710\u20100046 Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianping","family":"Chen","sequence":"additional","affiliation":[{"name":"State Key Laboratory Breeding Base for Zhejiang Sustainable Pest and Disease Control Ministry of Agriculture Key Laboratory of Biotechnology in Plant Protection Institute of Virology and Biotechnology Zhejiang Academy of Agricultural Sciences Hangzhou 310021 China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2013,3,4]]},"reference":[{"key":"e_1_2_6_2_1","first-page":"1139","volume-title":"Virus Taxonomy, Ninth Report of the International Committee on Taxonomy of Viruses","author":"Adams M.J.","year":"2011"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1094\/MPMI-18-0194"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1099\/vir.0.043513-0"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2005.04.012"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-313X.2005.02539.x"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M000618200"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.112408.134012"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1364-3703.2004.00246.x"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.78.14.7379-7391.2004"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tplants.2011.02.010"},{"key":"e_1_2_6_12_1","first-page":"685","article-title":"TopPred II: an improved software for membrane protein structure predictions","volume":"10","author":"Claros M.G.","year":"1994","journal-title":"Comput. 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