Evidence that Vector Transmission of a Plant Virus Requires Conformational Change in Virus Particles
Transmission of Cucumber necrosis virus (CNV) by zoospores of its fungal vector, Olpidium bornovanus, involves specific adsorption of virus particles onto the zoospore plasmalemma prior to infestation of cucumber roots by virus-bound zoospores. Previous work has shown that specific components of bot...
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| Veröffentlicht in: | Journal of molecular biology 2004-04, Vol.338 (3), p.507-517 |
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| creator | Kakani, Kishore Reade, Ron Rochon, D'Ann |
| description | Transmission of Cucumber necrosis virus (CNV) by zoospores of its fungal vector,
Olpidium bornovanus, involves specific adsorption of virus particles onto the zoospore plasmalemma prior to infestation of cucumber roots by virus-bound zoospores. Previous work has shown that specific components of both CNV and zoospores are required for successful CNV/zoospore recognition. Here, we show that limited trypsin digestion of CNV following
in vitro CNV/zoospore binding assays, results in the production of specific proteolytic digestion products under conditions where native CNV is resistant. The proteolytic digestion pattern of zoospore-bound CNV was found to be similar to that of swollen CNV particles produced
in vitro, suggesting that zoospore-bound CNV is in an altered conformational state, perhaps similar to that of swollen CNV. We show that an engineered CNV mutant (Pro73Gly) in which a conserved proline residue (Pro73) in the β-annulus of the CP
arm is changed to glycine is resistant to proteolysis following
in vitro zoospore binding assays. Moreover, Pro73Gly particles are transmitted only poorly by
O.
bornovanus
. Together, the results of these studies suggest that CNV undergoes conformational change upon zoospore binding and that the conformational change is important for CNV transmissibility. |
| doi_str_mv | 10.1016/j.jmb.2004.03.008 |
| format | Article |
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Olpidium bornovanus, involves specific adsorption of virus particles onto the zoospore plasmalemma prior to infestation of cucumber roots by virus-bound zoospores. Previous work has shown that specific components of both CNV and zoospores are required for successful CNV/zoospore recognition. Here, we show that limited trypsin digestion of CNV following
in vitro CNV/zoospore binding assays, results in the production of specific proteolytic digestion products under conditions where native CNV is resistant. The proteolytic digestion pattern of zoospore-bound CNV was found to be similar to that of swollen CNV particles produced
in vitro, suggesting that zoospore-bound CNV is in an altered conformational state, perhaps similar to that of swollen CNV. We show that an engineered CNV mutant (Pro73Gly) in which a conserved proline residue (Pro73) in the β-annulus of the CP
arm is changed to glycine is resistant to proteolysis following
in vitro zoospore binding assays. Moreover, Pro73Gly particles are transmitted only poorly by
O.
bornovanus
. Together, the results of these studies suggest that CNV undergoes conformational change upon zoospore binding and that the conformational change is important for CNV transmissibility.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2004.03.008</identifier><identifier>PMID: 15081809</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>coat protein arm domain ; conformational change ; Cucumber necrosis virus ; Cucumis sativus - microbiology ; Cucumis sativus - virology ; Fungi - metabolism ; Fungi - virology ; fungus transmission ; Mutation ; Olpidium bornovanus ; Plant Viruses - genetics ; Plant Viruses - physiology ; Protein Conformation ; Spores, Fungal - metabolism ; Spores, Fungal - virology ; tombusvirus ; Viral Proteins - chemistry ; Viral Proteins - genetics ; Viral Proteins - metabolism ; Virion - metabolism ; Virus Diseases - metabolism ; Virus Diseases - transmission</subject><ispartof>Journal of molecular biology, 2004-04, Vol.338 (3), p.507-517</ispartof><rights>2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-209b14099bf4ab09de173ae493aec0ed923158e6a3add5a4f3407a63e7f57de13</citedby><cites>FETCH-LOGICAL-c380t-209b14099bf4ab09de173ae493aec0ed923158e6a3add5a4f3407a63e7f57de13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jmb.2004.03.008$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15081809$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kakani, Kishore</creatorcontrib><creatorcontrib>Reade, Ron</creatorcontrib><creatorcontrib>Rochon, D'Ann</creatorcontrib><title>Evidence that Vector Transmission of a Plant Virus Requires Conformational Change in Virus Particles</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Transmission of Cucumber necrosis virus (CNV) by zoospores of its fungal vector,
Olpidium bornovanus, involves specific adsorption of virus particles onto the zoospore plasmalemma prior to infestation of cucumber roots by virus-bound zoospores. Previous work has shown that specific components of both CNV and zoospores are required for successful CNV/zoospore recognition. Here, we show that limited trypsin digestion of CNV following
in vitro CNV/zoospore binding assays, results in the production of specific proteolytic digestion products under conditions where native CNV is resistant. The proteolytic digestion pattern of zoospore-bound CNV was found to be similar to that of swollen CNV particles produced
in vitro, suggesting that zoospore-bound CNV is in an altered conformational state, perhaps similar to that of swollen CNV. We show that an engineered CNV mutant (Pro73Gly) in which a conserved proline residue (Pro73) in the β-annulus of the CP
arm is changed to glycine is resistant to proteolysis following
in vitro zoospore binding assays. Moreover, Pro73Gly particles are transmitted only poorly by
O.
bornovanus
. Together, the results of these studies suggest that CNV undergoes conformational change upon zoospore binding and that the conformational change is important for CNV transmissibility.</description><subject>coat protein arm domain</subject><subject>conformational change</subject><subject>Cucumber necrosis virus</subject><subject>Cucumis sativus - microbiology</subject><subject>Cucumis sativus - virology</subject><subject>Fungi - metabolism</subject><subject>Fungi - virology</subject><subject>fungus transmission</subject><subject>Mutation</subject><subject>Olpidium bornovanus</subject><subject>Plant Viruses - genetics</subject><subject>Plant Viruses - physiology</subject><subject>Protein Conformation</subject><subject>Spores, Fungal - metabolism</subject><subject>Spores, Fungal - virology</subject><subject>tombusvirus</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><subject>Virion - metabolism</subject><subject>Virus Diseases - metabolism</subject><subject>Virus Diseases - transmission</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctKxDAUhoMoOl4ewI1k5a71pOklxZUM4wUERUa3IU1ONUPbaNIO-PZmmAF3ukkW-c5Pzv8Rcs4gZcDKq1W66ps0A8hT4CmA2CMzBqJORMnFPpkBZFmSCV4ekeMQVgBQ8FwckiNWgGAC6hkxi7U1OGik44ca6Rvq0Xm69GoIvQ3BuoG6lir63KkhPls_BfqCX5P1GOjcDa3zvRojpjo6_1DDO1I77Lhn5UerOwyn5KBVXcCz3X1CXm8Xy_l98vh09zC_eUw0FzAmGdQNy6GumzZXDdQGWcUV5nU8NKCpM84KgaXiyphC5S3PoVIlx6otqgjzE3K5zf307mvCMMq4g8Yu_h3dFGTFRJaLKvsXjN0AML4B2RbU3oXgsZWf3vbKf0sGcuNArmR0IDcOJHAZHcSZi1341PRofid2pUfgegtg7GJt0cug7caBia3qURpn_4j_AY7Nl8I</recordid><startdate>20040430</startdate><enddate>20040430</enddate><creator>Kakani, Kishore</creator><creator>Reade, Ron</creator><creator>Rochon, D'Ann</creator><general>Elsevier Ltd</general><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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20040430</creationdate><title>Evidence that Vector Transmission of a Plant Virus Requires Conformational Change in Virus Particles</title><author>Kakani, Kishore ; Reade, Ron ; Rochon, D'Ann</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c380t-209b14099bf4ab09de173ae493aec0ed923158e6a3add5a4f3407a63e7f57de13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>coat protein arm domain</topic><topic>conformational change</topic><topic>Cucumber necrosis virus</topic><topic>Cucumis sativus - microbiology</topic><topic>Cucumis sativus - virology</topic><topic>Fungi - metabolism</topic><topic>Fungi - virology</topic><topic>fungus transmission</topic><topic>Mutation</topic><topic>Olpidium bornovanus</topic><topic>Plant Viruses - genetics</topic><topic>Plant Viruses - physiology</topic><topic>Protein Conformation</topic><topic>Spores, Fungal - metabolism</topic><topic>Spores, Fungal - virology</topic><topic>tombusvirus</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><topic>Virion - metabolism</topic><topic>Virus Diseases - metabolism</topic><topic>Virus Diseases - transmission</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kakani, Kishore</creatorcontrib><creatorcontrib>Reade, Ron</creatorcontrib><creatorcontrib>Rochon, D'Ann</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kakani, Kishore</au><au>Reade, Ron</au><au>Rochon, D'Ann</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence that Vector Transmission of a Plant Virus Requires Conformational Change in Virus Particles</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2004-04-30</date><risdate>2004</risdate><volume>338</volume><issue>3</issue><spage>507</spage><epage>517</epage><pages>507-517</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>Transmission of Cucumber necrosis virus (CNV) by zoospores of its fungal vector,
Olpidium bornovanus, involves specific adsorption of virus particles onto the zoospore plasmalemma prior to infestation of cucumber roots by virus-bound zoospores. Previous work has shown that specific components of both CNV and zoospores are required for successful CNV/zoospore recognition. Here, we show that limited trypsin digestion of CNV following
in vitro CNV/zoospore binding assays, results in the production of specific proteolytic digestion products under conditions where native CNV is resistant. The proteolytic digestion pattern of zoospore-bound CNV was found to be similar to that of swollen CNV particles produced
in vitro, suggesting that zoospore-bound CNV is in an altered conformational state, perhaps similar to that of swollen CNV. We show that an engineered CNV mutant (Pro73Gly) in which a conserved proline residue (Pro73) in the β-annulus of the CP
arm is changed to glycine is resistant to proteolysis following
in vitro zoospore binding assays. Moreover, Pro73Gly particles are transmitted only poorly by
O.
bornovanus
. Together, the results of these studies suggest that CNV undergoes conformational change upon zoospore binding and that the conformational change is important for CNV transmissibility.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>15081809</pmid><doi>10.1016/j.jmb.2004.03.008</doi><tpages>11</tpages></addata></record> |
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| subjects | coat protein arm domain conformational change Cucumber necrosis virus Cucumis sativus - microbiology Cucumis sativus - virology Fungi - metabolism Fungi - virology fungus transmission Mutation Olpidium bornovanus Plant Viruses - genetics Plant Viruses - physiology Protein Conformation Spores, Fungal - metabolism Spores, Fungal - virology tombusvirus Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - metabolism Virion - metabolism Virus Diseases - metabolism Virus Diseases - transmission |
| title | Evidence that Vector Transmission of a Plant Virus Requires Conformational Change in Virus Particles |
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