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...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1995
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| _version_ | 1797087945089351680 |
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| author | Brookman, J Stott, A Cheeseman, P Burns, N Adams, SE Kingsman, A Gull, K |
| author_facet | Brookman, J Stott, A Cheeseman, P Burns, N Adams, SE Kingsman, A Gull, K |
| author_sort | Brookman, J |
| collection | OXFORD |
| 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. |
| first_indexed | 2024-03-07T02:42:48Z |
| format | Journal article |
| id | oxford-uuid:ab070100-a7be-4cfa-ad94-205a711eb369 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:42:48Z |
| publishDate | 1995 |
| record_format | dspace |
| spelling | oxford-uuid:ab070100-a7be-4cfa-ad94-205a711eb3692022-03-27T03:19:10ZAn immunological analysis of Ty1 virus-like particle structure.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:ab070100-a7be-4cfa-ad94-205a711eb369EnglishSymplectic Elements at Oxford1995Brookman, JStott, ACheeseman, PBurns, NAdams, SEKingsman, AGull, KWe 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. |
| spellingShingle | Brookman, J Stott, A Cheeseman, P Burns, N Adams, SE Kingsman, A Gull, K An immunological analysis of Ty1 virus-like particle structure. |
| title | An immunological analysis of Ty1 virus-like particle structure. |
| title_full | An immunological analysis of Ty1 virus-like particle structure. |
| title_fullStr | An immunological analysis of Ty1 virus-like particle structure. |
| title_full_unstemmed | An immunological analysis of Ty1 virus-like particle structure. |
| title_short | An immunological analysis of Ty1 virus-like particle structure. |
| title_sort | immunological analysis of ty1 virus like particle structure |
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