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The interaction of Lolium latent virus major coat protein with ankyrin repeat protein NbANKr redirects it to chloroplasts and modulates virus infection
The Lolium latent virus (LoLV) major coat protein sequence contains a typical chloroplast transit peptide (cTP) domain. In infected Nicotiana benthamiana leaf tissue, LoLV coat proteins can be detected at the chloroplast. In transient expression, several N-terminal deletions of the CP sequence, incr...
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Published in: | Journal of general virology 2018-05, Vol.99 (5), p.730-742 |
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description | The Lolium latent virus (LoLV) major coat protein sequence contains a typical chloroplast transit peptide (cTP) domain. In infected Nicotiana benthamiana leaf tissue, LoLV coat proteins can be detected at the chloroplast. In transient expression, several N-terminal deletions of the CP sequence, increasing in length, result in disruption of the domain functionality, markedly affecting intracellular localization. A yeast two-hybrid-based study using LoLV CP as bait identified several potentially interacting Arabidopsis host proteins, most of them with chloroplast-linked pathways. One of them, an ankyrin repeat protein, was studied in detail. The N. benthamiana homologue (NbANKr) targets chloroplasts, is able to co-localize with LoLV CP at chloroplast membranes in transient expression and shows a robust interaction with LoLV CP in vivo by BiFC, which has been confirmed by yeast two-hybrid data. Silencing NbANKr genes in N. benthamiana plants, prior to challenging with LoLV by mechanical inoculation, affects LoLV infection, significantly reducing the level of viral RNA in young leaves, compared to levels in control plants, and suggesting an inhibition of virus movement. Silencing of NbANKr has no obvious effect on plant phenotype, but is able to interfere with LoLV infection, opening the way for a new strategy for virus infection control. |
doi_str_mv | 10.1099/jgv.0.001043 |
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In infected Nicotiana benthamiana leaf tissue, LoLV coat proteins can be detected at the chloroplast. In transient expression, several N-terminal deletions of the CP sequence, increasing in length, result in disruption of the domain functionality, markedly affecting intracellular localization. A yeast two-hybrid-based study using LoLV CP as bait identified several potentially interacting Arabidopsis host proteins, most of them with chloroplast-linked pathways. One of them, an ankyrin repeat protein, was studied in detail. The N. benthamiana homologue (NbANKr) targets chloroplasts, is able to co-localize with LoLV CP at chloroplast membranes in transient expression and shows a robust interaction with LoLV CP in vivo by BiFC, which has been confirmed by yeast two-hybrid data. Silencing NbANKr genes in N. benthamiana plants, prior to challenging with LoLV by mechanical inoculation, affects LoLV infection, significantly reducing the level of viral RNA in young leaves, compared to levels in control plants, and suggesting an inhibition of virus movement. 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In infected Nicotiana benthamiana leaf tissue, LoLV coat proteins can be detected at the chloroplast. In transient expression, several N-terminal deletions of the CP sequence, increasing in length, result in disruption of the domain functionality, markedly affecting intracellular localization. A yeast two-hybrid-based study using LoLV CP as bait identified several potentially interacting Arabidopsis host proteins, most of them with chloroplast-linked pathways. One of them, an ankyrin repeat protein, was studied in detail. The N. benthamiana homologue (NbANKr) targets chloroplasts, is able to co-localize with LoLV CP at chloroplast membranes in transient expression and shows a robust interaction with LoLV CP in vivo by BiFC, which has been confirmed by yeast two-hybrid data. Silencing NbANKr genes in N. benthamiana plants, prior to challenging with LoLV by mechanical inoculation, affects LoLV infection, significantly reducing the level of viral RNA in young leaves, compared to levels in control plants, and suggesting an inhibition of virus movement. Silencing of NbANKr has no obvious effect on plant phenotype, but is able to interfere with LoLV infection, opening the way for a new strategy for virus infection control.</description><subject>Ankyrin Repeat</subject><subject>Capsid Proteins - genetics</subject><subject>Chloroplast Proteins - genetics</subject><subject>Chloroplasts - virology</subject><subject>Gene Expression Regulation, Plant</subject><subject>Gene Silencing</subject><subject>Nicotiana - virology</subject><subject>Plant Diseases - virology</subject><subject>Plant Leaves - virology</subject><subject>Plant Proteins - genetics</subject><subject>Plant Viruses - genetics</subject><subject>Protein Sorting Signals - genetics</subject><subject>RNA, Viral - genetics</subject><subject>Two-Hybrid System Techniques</subject><issn>0022-1317</issn><issn>1465-2099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNpNkctOwzAQRS0EoqWwY428ZEGKH3kuq4qXqMqmrCPHGVOXJC62U9Qv4XdxaUGsRjNzdOdqLkKXlIwpKYrb1dtmTMaEUBLzIzSkcZpELCyO0ZAQxiLKaTZAZ86tAhPHSXaKBqxIkizL6BB9LZaAdefBCum16bBReGYa3be4ER46jzfa9g63YmUslkZ4vLbGg-7wp_ZLLLr3rQ2NhTX8282ryfzZhmmtLUjvsPbYGyyXjbFm3QgXRqKrcWvqfnfHHc7oTsGPj3N0okTj4OJQR-j1_m4xfYxmLw9P08kskpwVPmJSpZIoBQQKQmuR1YWQImVprPK65lmaV5wwKgUFyFlCWZUVQKWS4UN5ymI-Qtd73eD8owfny1Y7CU0jOjC9KxmhSc4Z5Tv0Zo9Ka5yzoMq11a2w25KSchdFGaIoSbmPIuBXB-W-aqH-g39_z78Bok2IdA</recordid><startdate>201805</startdate><enddate>201805</enddate><creator>Vaira, A M</creator><creator>Lim, H S</creator><creator>Bauchan, G</creator><creator>Gulbronson, C J</creator><creator>Miozzi, L</creator><creator>Vinals, N</creator><creator>Natilla, A</creator><creator>Hammond, J</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201805</creationdate><title>The interaction of Lolium latent virus major coat protein with ankyrin repeat protein NbANKr redirects it to chloroplasts and modulates virus infection</title><author>Vaira, A M ; Lim, H S ; Bauchan, G ; Gulbronson, C J ; Miozzi, L ; Vinals, N ; Natilla, A ; Hammond, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c329t-2cf6c0ffe0e901da7d9aca6264f8dd3768b3021ca1ee82512b79e1cfc20986243</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Ankyrin Repeat</topic><topic>Capsid Proteins - genetics</topic><topic>Chloroplast Proteins - genetics</topic><topic>Chloroplasts - virology</topic><topic>Gene Expression Regulation, Plant</topic><topic>Gene Silencing</topic><topic>Nicotiana - virology</topic><topic>Plant Diseases - virology</topic><topic>Plant Leaves - virology</topic><topic>Plant Proteins - genetics</topic><topic>Plant Viruses - genetics</topic><topic>Protein Sorting Signals - genetics</topic><topic>RNA, Viral - genetics</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vaira, A M</creatorcontrib><creatorcontrib>Lim, H S</creatorcontrib><creatorcontrib>Bauchan, G</creatorcontrib><creatorcontrib>Gulbronson, C J</creatorcontrib><creatorcontrib>Miozzi, L</creatorcontrib><creatorcontrib>Vinals, N</creatorcontrib><creatorcontrib>Natilla, A</creatorcontrib><creatorcontrib>Hammond, J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of general virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vaira, A M</au><au>Lim, H S</au><au>Bauchan, G</au><au>Gulbronson, C J</au><au>Miozzi, L</au><au>Vinals, N</au><au>Natilla, A</au><au>Hammond, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The interaction of Lolium latent virus major coat protein with ankyrin repeat protein NbANKr redirects it to chloroplasts and modulates virus infection</atitle><jtitle>Journal of general virology</jtitle><addtitle>J Gen Virol</addtitle><date>2018-05</date><risdate>2018</risdate><volume>99</volume><issue>5</issue><spage>730</spage><epage>742</epage><pages>730-742</pages><issn>0022-1317</issn><eissn>1465-2099</eissn><abstract>The Lolium latent virus (LoLV) major coat protein sequence contains a typical chloroplast transit peptide (cTP) domain. In infected Nicotiana benthamiana leaf tissue, LoLV coat proteins can be detected at the chloroplast. In transient expression, several N-terminal deletions of the CP sequence, increasing in length, result in disruption of the domain functionality, markedly affecting intracellular localization. A yeast two-hybrid-based study using LoLV CP as bait identified several potentially interacting Arabidopsis host proteins, most of them with chloroplast-linked pathways. One of them, an ankyrin repeat protein, was studied in detail. The N. benthamiana homologue (NbANKr) targets chloroplasts, is able to co-localize with LoLV CP at chloroplast membranes in transient expression and shows a robust interaction with LoLV CP in vivo by BiFC, which has been confirmed by yeast two-hybrid data. Silencing NbANKr genes in N. benthamiana plants, prior to challenging with LoLV by mechanical inoculation, affects LoLV infection, significantly reducing the level of viral RNA in young leaves, compared to levels in control plants, and suggesting an inhibition of virus movement. Silencing of NbANKr has no obvious effect on plant phenotype, but is able to interfere with LoLV infection, opening the way for a new strategy for virus infection control.</abstract><cop>England</cop><pmid>29557771</pmid><doi>10.1099/jgv.0.001043</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Ankyrin Repeat Capsid Proteins - genetics Chloroplast Proteins - genetics Chloroplasts - virology Gene Expression Regulation, Plant Gene Silencing Nicotiana - virology Plant Diseases - virology Plant Leaves - virology Plant Proteins - genetics Plant Viruses - genetics Protein Sorting Signals - genetics RNA, Viral - genetics Two-Hybrid System Techniques |
title | The interaction of Lolium latent virus major coat protein with ankyrin repeat protein NbANKr redirects it to chloroplasts and modulates virus infection |
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