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
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...
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| Veröffentlicht in: | Archives of virology 2008, Vol.153 (1), p.105-115 |
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| creator | Yambao, M. L. M Yagihashi, H Sekiguchi, H Sekiguchi, T Sasaki, T Sato, M Atsumi, G Tacahashi, Y Nakahara, K. S Uyeda, I |
| description | 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. |
| doi_str_mv | 10.1007/s00705-007-1073-3 |
| format | Article |
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L. M ; Yagihashi, H ; Sekiguchi, H ; Sekiguchi, T ; Sasaki, T ; Sato, M ; Atsumi, G ; Tacahashi, Y ; Nakahara, K. S ; Uyeda, I</creator><creatorcontrib>Yambao, M. L. M ; Yagihashi, H ; Sekiguchi, H ; Sekiguchi, T ; Sasaki, T ; Sato, M ; Atsumi, G ; Tacahashi, Y ; Nakahara, K. S ; Uyeda, I</creatorcontrib><description>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.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s00705-007-1073-3</identifier><identifier>PMID: 17955160</identifier><language>eng</language><publisher>Vienna: Vienna : Springer-Verlag</publisher><subject>Amino acid substitution ; Aspartic acid ; Beans ; Biological and medical sciences ; Biomedical and Life Sciences ; Biomedicine ; Carrier Proteins ; Cloning ; Clover yellow vein virus ; Cysteine Endopeptidases - chemistry ; Cysteine Endopeptidases - genetics ; Cysteine Endopeptidases - pharmacology ; Cysteine Endopeptidases - physiology ; Fundamental and applied biological sciences. Psychology ; Genomes ; Infections ; Infectious Diseases ; Isoleucine ; Medical Microbiology ; Microbiology ; Miscellaneous ; Mutants ; Mutation ; Necrosis ; Nicotiana - virology ; Nicotiana benthamiana ; Pathogens ; Plant Diseases - etiology ; Plant Diseases - virology ; Plant viruses ; Point Mutation ; Potyvirus - genetics ; Potyvirus - physiology ; Proteinase ; Proteins ; Ribonucleic acid ; RNA ; RNA Interference - drug effects ; RNA Interference - physiology ; RNA-mediated interference ; Suppression, Genetic - drug effects ; Suppression, Genetic - physiology ; Threonine ; Tumor Suppressor Proteins ; Tyrosine ; Vicia faba ; Vicia faba - virology ; Viral infections ; Viral Proteins - chemistry ; Viral Proteins - genetics ; Viral Proteins - metabolism ; Viral Proteins - pharmacology ; Viral Proteins - physiology ; Virology ; Virulence ; Viruses ; Zinc finger proteins</subject><ispartof>Archives of virology, 2008, Vol.153 (1), p.105-115</ispartof><rights>Springer-Verlag 2007</rights><rights>2008 INIST-CNRS</rights><rights>Springer-Verlag 2008</rights><rights>Springer-Verlag 2007.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c569t-9be75a706edb445f6ed7af6dc7fde01cb160bd324632f8216db054caefc1a6dc3</citedby><cites>FETCH-LOGICAL-c569t-9be75a706edb445f6ed7af6dc7fde01cb160bd324632f8216db054caefc1a6dc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00705-007-1073-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00705-007-1073-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,4009,27902,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20245997$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17955160$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yambao, M. L. M</creatorcontrib><creatorcontrib>Yagihashi, H</creatorcontrib><creatorcontrib>Sekiguchi, H</creatorcontrib><creatorcontrib>Sekiguchi, T</creatorcontrib><creatorcontrib>Sasaki, T</creatorcontrib><creatorcontrib>Sato, M</creatorcontrib><creatorcontrib>Atsumi, G</creatorcontrib><creatorcontrib>Tacahashi, Y</creatorcontrib><creatorcontrib>Nakahara, K. S</creatorcontrib><creatorcontrib>Uyeda, I</creatorcontrib><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</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><addtitle>Arch Virol</addtitle><description>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.</description><subject>Amino acid substitution</subject><subject>Aspartic acid</subject><subject>Beans</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Carrier Proteins</subject><subject>Cloning</subject><subject>Clover yellow vein virus</subject><subject>Cysteine Endopeptidases - chemistry</subject><subject>Cysteine Endopeptidases - genetics</subject><subject>Cysteine Endopeptidases - pharmacology</subject><subject>Cysteine Endopeptidases - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genomes</subject><subject>Infections</subject><subject>Infectious Diseases</subject><subject>Isoleucine</subject><subject>Medical Microbiology</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Necrosis</subject><subject>Nicotiana - virology</subject><subject>Nicotiana benthamiana</subject><subject>Pathogens</subject><subject>Plant Diseases - etiology</subject><subject>Plant Diseases - virology</subject><subject>Plant viruses</subject><subject>Point Mutation</subject><subject>Potyvirus - genetics</subject><subject>Potyvirus - physiology</subject><subject>Proteinase</subject><subject>Proteins</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA Interference - drug effects</subject><subject>RNA Interference - physiology</subject><subject>RNA-mediated interference</subject><subject>Suppression, Genetic - drug effects</subject><subject>Suppression, Genetic - physiology</subject><subject>Threonine</subject><subject>Tumor Suppressor Proteins</subject><subject>Tyrosine</subject><subject>Vicia faba</subject><subject>Vicia faba - virology</subject><subject>Viral infections</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><subject>Viral Proteins - pharmacology</subject><subject>Viral Proteins - physiology</subject><subject>Virology</subject><subject>Virulence</subject><subject>Viruses</subject><subject>Zinc finger proteins</subject><issn>0304-8608</issn><issn>1432-8798</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kdtu1DAQhiMEokvhAbgBCwR3AR_iOLmsKk5SBQjodeQ4k11XiZ3azpZ9Ml6PCVm1EhLceKz5vznYf5Y9ZfQNo1S9jXhQmeOZM6pELu5lG1YInleqru5nGypokVclrU6yRzFeUYoJIR9mJ0zVUrKSbrJfX711iYxz0sl6F4l1ZAfDBIEYP07eAapT8Al0BOJ7Yga_R_EAw-BvyB6Q39swR6IDEB2jN1Yn6MiNTTuSdphLCdz8p_tS_-3zWR7tAM5YtyVxnqYAMS6iNsnubToQ7ToSD-OU_Ejg562Ok9rgdUda0O5x9qDXQ4Qnx3iaXb5_9-P8Y37x5cOn87OL3MiyTnndgpJa0RK6tihkj1HpvuyM6jugzLT4CW0neFEK3leclV1LZWE09IZpxMRp9nrti39wPUNMzWijwcdrB36ODacllUwVCL78C7zyc3C4W8PLWpaFqGuK1It_UowLJXmlEGIrZIKPMUDfTMGOOhwaRpvF-GY1vlmui_GNwJpnx8ZzO0J3V3F0GoFXR0BHo4c-aHQg3nKc8kLW9TKcr1xEyW0h3G34v-nP16Je-0ZvAza-_M4pE5RWhRII_QYSyNNr</recordid><startdate>2008</startdate><enddate>2008</enddate><creator>Yambao, M. 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L. M ; Yagihashi, H ; Sekiguchi, H ; Sekiguchi, T ; Sasaki, T ; Sato, M ; Atsumi, G ; Tacahashi, Y ; Nakahara, K. S ; Uyeda, I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c569t-9be75a706edb445f6ed7af6dc7fde01cb160bd324632f8216db054caefc1a6dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino acid substitution</topic><topic>Aspartic acid</topic><topic>Beans</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Carrier Proteins</topic><topic>Cloning</topic><topic>Clover yellow vein virus</topic><topic>Cysteine Endopeptidases - chemistry</topic><topic>Cysteine Endopeptidases - genetics</topic><topic>Cysteine Endopeptidases - pharmacology</topic><topic>Cysteine Endopeptidases - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genomes</topic><topic>Infections</topic><topic>Infectious Diseases</topic><topic>Isoleucine</topic><topic>Medical Microbiology</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Necrosis</topic><topic>Nicotiana - virology</topic><topic>Nicotiana benthamiana</topic><topic>Pathogens</topic><topic>Plant Diseases - etiology</topic><topic>Plant Diseases - virology</topic><topic>Plant viruses</topic><topic>Point Mutation</topic><topic>Potyvirus - genetics</topic><topic>Potyvirus - physiology</topic><topic>Proteinase</topic><topic>Proteins</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>RNA Interference - drug effects</topic><topic>RNA Interference - physiology</topic><topic>RNA-mediated interference</topic><topic>Suppression, Genetic - drug effects</topic><topic>Suppression, Genetic - physiology</topic><topic>Threonine</topic><topic>Tumor Suppressor Proteins</topic><topic>Tyrosine</topic><topic>Vicia faba</topic><topic>Vicia faba - virology</topic><topic>Viral infections</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><topic>Viral Proteins - pharmacology</topic><topic>Viral Proteins - physiology</topic><topic>Virology</topic><topic>Virulence</topic><topic>Viruses</topic><topic>Zinc finger proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yambao, M. 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L. M</au><au>Yagihashi, H</au><au>Sekiguchi, H</au><au>Sekiguchi, T</au><au>Sasaki, T</au><au>Sato, M</au><au>Atsumi, G</au><au>Tacahashi, Y</au><au>Nakahara, K. S</au><au>Uyeda, I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>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</atitle><jtitle>Archives of virology</jtitle><stitle>Arch Virol</stitle><addtitle>Arch Virol</addtitle><date>2008</date><risdate>2008</risdate><volume>153</volume><issue>1</issue><spage>105</spage><epage>115</epage><pages>105-115</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><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.</abstract><cop>Vienna</cop><pub>Vienna : Springer-Verlag</pub><pmid>17955160</pmid><doi>10.1007/s00705-007-1073-3</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Archives of virology, 2008, Vol.153 (1), p.105-115 |
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| subjects | Amino acid substitution Aspartic acid Beans Biological and medical sciences Biomedical and Life Sciences Biomedicine Carrier Proteins Cloning Clover yellow vein virus Cysteine Endopeptidases - chemistry Cysteine Endopeptidases - genetics Cysteine Endopeptidases - pharmacology Cysteine Endopeptidases - physiology Fundamental and applied biological sciences. Psychology Genomes Infections Infectious Diseases Isoleucine Medical Microbiology Microbiology Miscellaneous Mutants Mutation Necrosis Nicotiana - virology Nicotiana benthamiana Pathogens Plant Diseases - etiology Plant Diseases - virology Plant viruses Point Mutation Potyvirus - genetics Potyvirus - physiology Proteinase Proteins Ribonucleic acid RNA RNA Interference - drug effects RNA Interference - physiology RNA-mediated interference Suppression, Genetic - drug effects Suppression, Genetic - physiology Threonine Tumor Suppressor Proteins Tyrosine Vicia faba Vicia faba - virology Viral infections Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - metabolism Viral Proteins - pharmacology Viral Proteins - physiology Virology Virulence Viruses Zinc finger proteins |
| 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 |
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