Studies of Coat Protein-Mediated Resistance to TMV: I. The PM2 Assembly Defective Mutant Confers Resistance to TMV
Tobacco mosaic virus mutant PM2 contains two amino acid changes in coat protein sequence relative to the sequence of the coat protein of TMV U1. This results in unstable infectivity, inability to cause normal systemic infection, and accumulation of elongated open helixes of coat protein. Using site-...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1995-04, Vol.208 (2), p.485-491 |
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| container_end_page | 491 |
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| container_title | Virology (New York, N.Y.) |
| container_volume | 208 |
| creator | Clark, W.Gregg Fitchen, John H. Beachy, Roger N. |
| description | Tobacco mosaic virus mutant PM2 contains two amino acid changes in coat protein sequence relative to the sequence of the coat protein of TMV U1. This results in unstable infectivity, inability to cause normal systemic infection, and accumulation of elongated open helixes of coat protein. Using site-directed mutagenesis we demonstrated that the characteristics of PM2 are due to the change of Thr28 → Ile, while the second change, Glu95 → Asp, had no apparent effect on virion structure or infectivity. Transgenic Nicotiana tabacum cv Xanthi NN and Xanthi nn plants that accumulate coat protein that contains one or both of the amino acid changes are as resistant to TMV infection as transgenic plants that contain wildtype TMV coat protein. The implication of these results on a model for coat protein-mediated resistance that involves the interaction of transgenic coat protein with the challenge virus is discussed. |
| doi_str_mv | 10.1006/viro.1995.1179 |
| format | Article |
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Transgenic Nicotiana tabacum cv Xanthi NN and Xanthi nn plants that accumulate coat protein that contains one or both of the amino acid changes are as resistant to TMV infection as transgenic plants that contain wildtype TMV coat protein. The implication of these results on a model for coat protein-mediated resistance that involves the interaction of transgenic coat protein with the challenge virus is discussed.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1006/viro.1995.1179</identifier><identifier>PMID: 7747421</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acids ; Base Sequence ; Capsid - chemistry ; Capsid - genetics ; Genes, Viral - genetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Nicotiana - virology ; Plant Leaves - virology ; Plants, Genetically Modified ; Plants, Toxic ; Protein Conformation ; tobacco mosaic virus ; Tobacco Mosaic Virus - genetics ; Tobacco Mosaic Virus - pathogenicity ; Viral Structural Proteins - genetics ; Virion - genetics ; Virion - ultrastructure</subject><ispartof>Virology (New York, N.Y.), 1995-04, Vol.208 (2), p.485-491</ispartof><rights>1995 Academic Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/viro.1995.1179$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>315,781,785,3551,27928,27929,45999</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7747421$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Clark, W.Gregg</creatorcontrib><creatorcontrib>Fitchen, John H.</creatorcontrib><creatorcontrib>Beachy, Roger N.</creatorcontrib><title>Studies of Coat Protein-Mediated Resistance to TMV: I. The PM2 Assembly Defective Mutant Confers Resistance to TMV</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Tobacco mosaic virus mutant PM2 contains two amino acid changes in coat protein sequence relative to the sequence of the coat protein of TMV U1. This results in unstable infectivity, inability to cause normal systemic infection, and accumulation of elongated open helixes of coat protein. Using site-directed mutagenesis we demonstrated that the characteristics of PM2 are due to the change of Thr28 → Ile, while the second change, Glu95 → Asp, had no apparent effect on virion structure or infectivity. Transgenic Nicotiana tabacum cv Xanthi NN and Xanthi nn plants that accumulate coat protein that contains one or both of the amino acid changes are as resistant to TMV infection as transgenic plants that contain wildtype TMV coat protein. The implication of these results on a model for coat protein-mediated resistance that involves the interaction of transgenic coat protein with the challenge virus is discussed.</description><subject>Amino Acids</subject><subject>Base Sequence</subject><subject>Capsid - chemistry</subject><subject>Capsid - genetics</subject><subject>Genes, Viral - genetics</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Nicotiana - virology</subject><subject>Plant Leaves - virology</subject><subject>Plants, Genetically Modified</subject><subject>Plants, Toxic</subject><subject>Protein Conformation</subject><subject>tobacco mosaic virus</subject><subject>Tobacco Mosaic Virus - genetics</subject><subject>Tobacco Mosaic Virus - pathogenicity</subject><subject>Viral Structural Proteins - genetics</subject><subject>Virion - genetics</subject><subject>Virion - ultrastructure</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkc1PwzAMxSMEGmNw5YaUE7cWp2mThhsaX5M2McHgGqWtK4K2dSTppP33ZNpunCzLz09-_hFyzSBlAOJua12XMqWKlDGpTsiQgRIJ8JydkiFAniWizLJzcuH9D8ReShiQgZS5zDM2JO4j9I1FT7uWjjsT6Nx1Ae06mWFjTcCGvqO3Pph1jTR0dDH7uqeTlC6-kc5nGX3wHlfVckcfscU62C3SWR_VIbqtW3T-__4lOWvN0uPVsY7I5_PTYvyaTN9eJuOHaYIZsJBUFSBDxUFCWTNRVkK1vClEZkpuCgMxZ6FayXMDqhJ1rdqyRBQ8bxivatPyEbk9-G5c99ujD3plfY3LpVlj13vNhFSQFUUU3hyFfbXCRm-cXRm308cnxXl5mGO8dmvRaV9bjIEa62Jm3XRWM9B7HHqPQ-9x6D0O_gdzxHuA</recordid><startdate>19950420</startdate><enddate>19950420</enddate><creator>Clark, W.Gregg</creator><creator>Fitchen, John H.</creator><creator>Beachy, Roger N.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QO</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope></search><sort><creationdate>19950420</creationdate><title>Studies of Coat Protein-Mediated Resistance to TMV: I. 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The PM2 Assembly Defective Mutant Confers Resistance to TMV</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>1995-04-20</date><risdate>1995</risdate><volume>208</volume><issue>2</issue><spage>485</spage><epage>491</epage><pages>485-491</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Tobacco mosaic virus mutant PM2 contains two amino acid changes in coat protein sequence relative to the sequence of the coat protein of TMV U1. This results in unstable infectivity, inability to cause normal systemic infection, and accumulation of elongated open helixes of coat protein. Using site-directed mutagenesis we demonstrated that the characteristics of PM2 are due to the change of Thr28 → Ile, while the second change, Glu95 → Asp, had no apparent effect on virion structure or infectivity. Transgenic Nicotiana tabacum cv Xanthi NN and Xanthi nn plants that accumulate coat protein that contains one or both of the amino acid changes are as resistant to TMV infection as transgenic plants that contain wildtype TMV coat protein. The implication of these results on a model for coat protein-mediated resistance that involves the interaction of transgenic coat protein with the challenge virus is discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7747421</pmid><doi>10.1006/viro.1995.1179</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0042-6822 |
| ispartof | Virology (New York, N.Y.), 1995-04, Vol.208 (2), p.485-491 |
| issn | 0042-6822 1096-0341 |
| language | eng |
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| source | Elektronische Zeitschriftenbibliothek (Open access); MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acids Base Sequence Capsid - chemistry Capsid - genetics Genes, Viral - genetics Molecular Sequence Data Mutagenesis, Site-Directed Mutation Nicotiana - virology Plant Leaves - virology Plants, Genetically Modified Plants, Toxic Protein Conformation tobacco mosaic virus Tobacco Mosaic Virus - genetics Tobacco Mosaic Virus - pathogenicity Viral Structural Proteins - genetics Virion - genetics Virion - ultrastructure |
| title | Studies of Coat Protein-Mediated Resistance to TMV: I. The PM2 Assembly Defective Mutant Confers Resistance to TMV |
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