Substitution of a single amino acid in the 2b protein of Pea early-browning virus affects nematode transmission
The 2b protein of Pea early-browning virus (PEBV) is required for transmission of the virus by nematodes. Comparison of the 2b proteins of highly transmissible (TpA56) and poorly transmissible (SP5) isolates of PEBV identified two amino acid substitutions (G90S and G177R) that might be responsible f...
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| Veröffentlicht in: | Journal of general virology 2002-07, Vol.83 (7), p.1771-1775 |
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| container_title | Journal of general virology |
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| creator | Vellios, E Brown, D.J.F MacFarlane, S.A |
| description | The 2b protein of Pea early-browning virus (PEBV) is required for transmission of the virus by nematodes. Comparison of the 2b proteins of highly transmissible (TpA56) and poorly transmissible (SP5) isolates of PEBV identified two amino acid substitutions (G90S and G177R) that might be responsible for the poor transmission of isolate SP5. Hybrid viruses were created in which the TpA56 2b protein carried SP5-specific substitutions at residue 90 or 177, and in which the SP5 2b protein carried TpA56-specific substitutions at these positions. Transmission tests showed that the G177R substitution is sufficient to prevent nematode transmission of the virus. Examination of the 2b proteins from PEBV and other tobraviruses predicted the presence of a coiled-coil domain in the central region of the protein. This structural element is important for the association of interacting proteins and, thus, might mediate interaction of the 2b protein with the virus coat protein or with the vector nematode. |
| doi_str_mv | 10.1099/0022-1317-83-7-1771 |
| format | Article |
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Comparison of the 2b proteins of highly transmissible (TpA56) and poorly transmissible (SP5) isolates of PEBV identified two amino acid substitutions (G90S and G177R) that might be responsible for the poor transmission of isolate SP5. Hybrid viruses were created in which the TpA56 2b protein carried SP5-specific substitutions at residue 90 or 177, and in which the SP5 2b protein carried TpA56-specific substitutions at these positions. Transmission tests showed that the G177R substitution is sufficient to prevent nematode transmission of the virus. Examination of the 2b proteins from PEBV and other tobraviruses predicted the presence of a coiled-coil domain in the central region of the protein. 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Comparison of the 2b proteins of highly transmissible (TpA56) and poorly transmissible (SP5) isolates of PEBV identified two amino acid substitutions (G90S and G177R) that might be responsible for the poor transmission of isolate SP5. Hybrid viruses were created in which the TpA56 2b protein carried SP5-specific substitutions at residue 90 or 177, and in which the SP5 2b protein carried TpA56-specific substitutions at these positions. Transmission tests showed that the G177R substitution is sufficient to prevent nematode transmission of the virus. Examination of the 2b proteins from PEBV and other tobraviruses predicted the presence of a coiled-coil domain in the central region of the protein. This structural element is important for the association of interacting proteins and, thus, might mediate interaction of the 2b protein with the virus coat protein or with the vector nematode.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution</subject><subject>amino acids</subject><subject>Animals</subject><subject>coat proteins</subject><subject>Genome, Viral</subject><subject>hybrids</subject><subject>Molecular Sequence Data</subject><subject>Nematoda</subject><subject>Pea early-browning virus</subject><subject>Plant Diseases - virology</subject><subject>Plant Viruses - chemistry</subject><subject>Plant Viruses - genetics</subject><subject>protein-protein interactions</subject><subject>RNA Viruses - chemistry</subject><subject>RNA Viruses - genetics</subject><subject>Sequence Alignment</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - genetics</subject><subject>virus transmission</subject><subject>viruses</subject><issn>0022-1317</issn><issn>1465-2099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkMtuFDEQRS1ERCaBL0ACr1A2Ji7b_fASRbykSEQKWVt2d3nGqLsdbHei_H08zAhY1aLOvVU6hLwF_hG41pecC8FAQsd6yToGXQcvyAZU2zBR9y_J5i9xSs5y_sU5KNV0r8gpCN41XPcbEm9Xl0soawlxodFTS3NYthNSO4clUjuEkYaFlh1S4eh9igXDH_AGLUWbpifmUnxcaog-hLRmar3HoWS64GxLHJGWZJc8h5zridfkxNsp45vjPCd3Xz7_vPrGrn98_X716ZoNisvCWjG6Xo1aS--GZlSIWlrX9C3AqAYQTrWovG69A23H3gEI0QkAr1EplL08Jx8OvfXj3yvmYuoDA06TXTCu2XTQy1YBr6A8gEOKOSf05j6F2aYnA9zsPZu9RbO3aHppOrP3XFPvjvWrm3H8lzmKrcDFAdiF7e4xJDRbXOZQj7gQTRX1f9f7A-ptNHabQjZ3t4JDy3ktayTIZxGQkOA</recordid><startdate>20020701</startdate><enddate>20020701</enddate><creator>Vellios, E</creator><creator>Brown, D.J.F</creator><creator>MacFarlane, S.A</creator><general>Soc General Microbiol</general><scope>FBQ</scope><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>20020701</creationdate><title>Substitution of a single amino acid in the 2b protein of Pea early-browning virus affects nematode transmission</title><author>Vellios, E ; Brown, D.J.F ; MacFarlane, S.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c403t-62db84d993fbc5d4ee93ab58611d4c12b46e4f96fb19ad8b11227211f9e44e383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acid Substitution</topic><topic>amino acids</topic><topic>Animals</topic><topic>coat proteins</topic><topic>Genome, Viral</topic><topic>hybrids</topic><topic>Molecular Sequence Data</topic><topic>Nematoda</topic><topic>Pea early-browning virus</topic><topic>Plant Diseases - virology</topic><topic>Plant Viruses - chemistry</topic><topic>Plant Viruses - genetics</topic><topic>protein-protein interactions</topic><topic>RNA Viruses - chemistry</topic><topic>RNA Viruses - genetics</topic><topic>Sequence Alignment</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><topic>virus transmission</topic><topic>viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vellios, E</creatorcontrib><creatorcontrib>Brown, D.J.F</creatorcontrib><creatorcontrib>MacFarlane, S.A</creatorcontrib><collection>AGRIS</collection><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>Vellios, E</au><au>Brown, D.J.F</au><au>MacFarlane, S.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substitution of a single amino acid in the 2b protein of Pea early-browning virus affects nematode transmission</atitle><jtitle>Journal of general virology</jtitle><addtitle>J Gen Virol</addtitle><date>2002-07-01</date><risdate>2002</risdate><volume>83</volume><issue>7</issue><spage>1771</spage><epage>1775</epage><pages>1771-1775</pages><issn>0022-1317</issn><eissn>1465-2099</eissn><abstract>The 2b protein of Pea early-browning virus (PEBV) is required for transmission of the virus by nematodes. Comparison of the 2b proteins of highly transmissible (TpA56) and poorly transmissible (SP5) isolates of PEBV identified two amino acid substitutions (G90S and G177R) that might be responsible for the poor transmission of isolate SP5. Hybrid viruses were created in which the TpA56 2b protein carried SP5-specific substitutions at residue 90 or 177, and in which the SP5 2b protein carried TpA56-specific substitutions at these positions. Transmission tests showed that the G177R substitution is sufficient to prevent nematode transmission of the virus. Examination of the 2b proteins from PEBV and other tobraviruses predicted the presence of a coiled-coil domain in the central region of the protein. This structural element is important for the association of interacting proteins and, thus, might mediate interaction of the 2b protein with the virus coat protein or with the vector nematode.</abstract><cop>England</cop><pub>Soc General Microbiol</pub><pmid>12075098</pmid><doi>10.1099/0022-1317-83-7-1771</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino Acid Substitution amino acids Animals coat proteins Genome, Viral hybrids Molecular Sequence Data Nematoda Pea early-browning virus Plant Diseases - virology Plant Viruses - chemistry Plant Viruses - genetics protein-protein interactions RNA Viruses - chemistry RNA Viruses - genetics Sequence Alignment Viral Proteins - chemistry Viral Proteins - genetics virus transmission viruses |
| title | Substitution of a single amino acid in the 2b protein of Pea early-browning virus affects nematode transmission |
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