An Immunological Analysis of Ty1 Virus-like Particle Structure
We present an immunological characterization of the Ty1 virus-like particle (VLP). A panel of monoclonal and polyclonal antibodies were raised against the TYA particle-forming protein. Using these antibodies in epitope availability assays two N-terminal regions of the TYA protein were mapped project...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1995-02, Vol.207 (1), p.59-67 |
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| container_end_page | 67 |
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| container_title | Virology (New York, N.Y.) |
| container_volume | 207 |
| creator | Brookman, Jayne L. Stott, Andrew J. Cheeseman, Philip J. Burns, Nigel R. Adams, Sally E. Kingsman, Alan J. Gull, K. |
| description | We present an immunological characterization of the Ty1 virus-like particle (VLP). A panel of monoclonal and polyclonal antibodies were raised against the TYA particle-forming protein. Using these antibodies in epitope availability assays two N-terminal regions of the TYA protein were mapped projecting from or at the surface of the proteinaceous shell of the VLP. Two different C-termini of the TYA protein, corresponding to the C-terminus of the full-length and truncated forms, were seen to be buried within the particle core and not available for antibody binding. RNase accessibility studies demonstrated a difference in the porosity of the protein shell surrounding the Ty1 nucleic acid between different particle types, suggesting differences in subunit organization. |
| doi_str_mv | 10.1006/viro.1995.1051 |
| format | Article |
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RNase accessibility studies demonstrated a difference in the porosity of the protein shell surrounding the Ty1 nucleic acid between different particle types, suggesting differences in subunit organization.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1006/viro.1995.1051</identifier><identifier>PMID: 7532885</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Antibodies, Monoclonal ; Antibodies, Viral ; Base Sequence ; Endoribonucleases ; Epitopes - analysis ; Models, Biological ; Molecular Sequence Data ; Retroelements - immunology ; Retroelements - physiology ; Retroviridae - immunology ; Retroviridae - physiology ; Retroviridae - ultrastructure ; RNA, Viral - metabolism ; Viral Proteins - analysis ; Viral Proteins - immunology ; Virion - immunology ; Virion - ultrastructure</subject><ispartof>Virology (New York, N.Y.), 1995-02, Vol.207 (1), p.59-67</ispartof><rights>1995 Academic Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c410t-8b886b5f63ac295ce12e3be4a53c99237ce580e81ec055d3e4b044277a789cf23</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/viro.1995.1051$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7532885$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brookman, Jayne L.</creatorcontrib><creatorcontrib>Stott, Andrew J.</creatorcontrib><creatorcontrib>Cheeseman, Philip J.</creatorcontrib><creatorcontrib>Burns, Nigel R.</creatorcontrib><creatorcontrib>Adams, Sally E.</creatorcontrib><creatorcontrib>Kingsman, Alan J.</creatorcontrib><creatorcontrib>Gull, K.</creatorcontrib><title>An Immunological Analysis of Ty1 Virus-like Particle Structure</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>We present an immunological characterization of the Ty1 virus-like particle (VLP). A panel of monoclonal and polyclonal antibodies were raised against the TYA particle-forming protein. Using these antibodies in epitope availability assays two N-terminal regions of the TYA protein were mapped projecting from or at the surface of the proteinaceous shell of the VLP. Two different C-termini of the TYA protein, corresponding to the C-terminus of the full-length and truncated forms, were seen to be buried within the particle core and not available for antibody binding. RNase accessibility studies demonstrated a difference in the porosity of the protein shell surrounding the Ty1 nucleic acid between different particle types, suggesting differences in subunit organization.</description><subject>Amino Acid Sequence</subject><subject>Antibodies, Monoclonal</subject><subject>Antibodies, Viral</subject><subject>Base Sequence</subject><subject>Endoribonucleases</subject><subject>Epitopes - analysis</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>Retroelements - immunology</subject><subject>Retroelements - physiology</subject><subject>Retroviridae - immunology</subject><subject>Retroviridae - physiology</subject><subject>Retroviridae - ultrastructure</subject><subject>RNA, Viral - metabolism</subject><subject>Viral Proteins - analysis</subject><subject>Viral Proteins - immunology</subject><subject>Virion - immunology</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>eNqFkEtLw0AUhQdRaq1u3QlZuUudR-aRjVDER6GgYHU7TCY3Mppk6kxS6L83ocWduLocznfP4kPokuA5wVjcbF3wc5LnfIicHKEpwblIMcvIMZpinNFUKEpP0VmMn3jIUuIJmkjOqFJ8im4XbbJsmr71tf9w1tTJojX1LrqY-CpZ70jy7kIf09p9QfJiQudsDclrF3rb9QHO0Ull6ggXhztDbw_367undPX8uLxbrFKbEdylqlBKFLwSzFiacwuEAisgM5zZPKdMWuAKgyJgMeclg6zAWUalNFLltqJshq73u5vgv3uInW5ctFDXpgXfRy0l4ZIp9S9IhJSCihGc70EbfIwBKr0JrjFhpwnWo1k9mtWjWT2aHR6uDst90UD5ix9UDr3a9zB42DoIOloHrYXSBbCdLr37a_oH8_WGow</recordid><startdate>19950220</startdate><enddate>19950220</enddate><creator>Brookman, Jayne L.</creator><creator>Stott, Andrew J.</creator><creator>Cheeseman, Philip J.</creator><creator>Burns, Nigel R.</creator><creator>Adams, Sally E.</creator><creator>Kingsman, Alan J.</creator><creator>Gull, K.</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>AAYXX</scope><scope>CITATION</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19950220</creationdate><title>An Immunological Analysis of Ty1 Virus-like Particle Structure</title><author>Brookman, Jayne L. ; 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| identifier | ISSN: 0042-6822 |
| ispartof | Virology (New York, N.Y.), 1995-02, Vol.207 (1), p.59-67 |
| issn | 0042-6822 1096-0341 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77157388 |
| source | MEDLINE; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals |
| subjects | Amino Acid Sequence Antibodies, Monoclonal Antibodies, Viral Base Sequence Endoribonucleases Epitopes - analysis Models, Biological Molecular Sequence Data Retroelements - immunology Retroelements - physiology Retroviridae - immunology Retroviridae - physiology Retroviridae - ultrastructure RNA, Viral - metabolism Viral Proteins - analysis Viral Proteins - immunology Virion - immunology Virion - ultrastructure |
| title | An Immunological Analysis of Ty1 Virus-like Particle Structure |
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