Analysis of the Epitope Structure of Plum pox virus Coat Protein
Typing of the particular Plum pox virus (PPV) strain responsible in an outbreak has important practical implications and is frequently performed using strain-specific monoclonal antibodies (MAbs). Analysis in Western blots of the reactivity of 24 MAbs to a 112-amino-acid N-terminal fragment of the P...
| Main Authors: | , , , , , , |
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| Format: | article |
| Language: | Inglés |
| Published: |
2017
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| Online Access: | http://hdl.handle.net/20.500.11939/4947 |
| _version_ | 1855032200937865216 |
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| author | Candresse, Thierry Saenz, Pilar Garcia, Juan Antonio Boscia, Donato Navratil, Milan Gorris, María T. Cambra, Mariano |
| author_browse | Boscia, Donato Cambra, Mariano Candresse, Thierry Garcia, Juan Antonio Gorris, María T. Navratil, Milan Saenz, Pilar |
| author_facet | Candresse, Thierry Saenz, Pilar Garcia, Juan Antonio Boscia, Donato Navratil, Milan Gorris, María T. Cambra, Mariano |
| author_sort | Candresse, Thierry |
| collection | ReDivia |
| description | Typing of the particular Plum pox virus (PPV) strain responsible in an outbreak has important practical implications and is frequently performed using strain-specific monoclonal antibodies (MAbs). Analysis in Western blots of the reactivity of 24 MAbs to a 112-amino-acid N-terminal fragment of the PPV coat protein (CP) expressed in Escherichia coli showed that 21 of the 24 MAbs recognized linear or denaturation-insensitive epitopes. A series of eight C-truncated CP fragments allowed the mapping of the epitopes recognized by the MAbs. In all, 14 of them reacted to the N-terminal hypervariable region, defining a minimum of six epitopes, while 7 reacted to the beginning of the core region, defining a minimum of three epitopes. Sequence comparisons allowed the more precise positioning of regions recognized by several MAbs, including those recognized by the 5B-IV1A universal MAb (amino acids 94 to 100) and by the 4DG5 and 4DG11 D serogroup-specific MAbs (amino acids 43 to 64). A similar approach coupled with infectious cDNA clone mutagenesis showed that a V74T mutation in the N-terminus of the CP abolished the binding of the M serogroup-specific AL MAb. Taken together, these results provide a detailed positioning of the epitopes recognized by the most widely used PPV detection and typing MAbs. |
| format | article |
| id | ReDivia4947 |
| institution | Instituto Valenciano de Investigaciones Agrarias (IVIA) |
| language | Inglés |
| publishDate | 2017 |
| publishDateRange | 2017 |
| publishDateSort | 2017 |
| record_format | dspace |
| spelling | ReDivia49472025-04-25T14:44:59Z Analysis of the Epitope Structure of Plum pox virus Coat Protein Candresse, Thierry Saenz, Pilar Garcia, Juan Antonio Boscia, Donato Navratil, Milan Gorris, María T. Cambra, Mariano Typing of the particular Plum pox virus (PPV) strain responsible in an outbreak has important practical implications and is frequently performed using strain-specific monoclonal antibodies (MAbs). Analysis in Western blots of the reactivity of 24 MAbs to a 112-amino-acid N-terminal fragment of the PPV coat protein (CP) expressed in Escherichia coli showed that 21 of the 24 MAbs recognized linear or denaturation-insensitive epitopes. A series of eight C-truncated CP fragments allowed the mapping of the epitopes recognized by the MAbs. In all, 14 of them reacted to the N-terminal hypervariable region, defining a minimum of six epitopes, while 7 reacted to the beginning of the core region, defining a minimum of three epitopes. Sequence comparisons allowed the more precise positioning of regions recognized by several MAbs, including those recognized by the 5B-IV1A universal MAb (amino acids 94 to 100) and by the 4DG5 and 4DG11 D serogroup-specific MAbs (amino acids 43 to 64). A similar approach coupled with infectious cDNA clone mutagenesis showed that a V74T mutation in the N-terminus of the CP abolished the binding of the M serogroup-specific AL MAb. Taken together, these results provide a detailed positioning of the epitopes recognized by the most widely used PPV detection and typing MAbs. 2017-06-01T10:11:24Z 2017-06-01T10:11:24Z 2011 MAY 2011 article publishedVersion Candresse, Thierry, Saenz, P., A. Garcia, J., Boscia, Donato, Navratil, Milan, Teresa Gorris, M., Cambra, M. (2011). Analysis of the Epitope Structure of Plum pox virus Coat Protein. Phytopathology, 101(5), 611-619. 0031-949X http://hdl.handle.net/20.500.11939/4947 10.1094/PHYTO-10-10-0274 en openAccess Impreso |
| spellingShingle | Candresse, Thierry Saenz, Pilar Garcia, Juan Antonio Boscia, Donato Navratil, Milan Gorris, María T. Cambra, Mariano Analysis of the Epitope Structure of Plum pox virus Coat Protein |
| title | Analysis of the Epitope Structure of Plum pox virus Coat Protein |
| title_full | Analysis of the Epitope Structure of Plum pox virus Coat Protein |
| title_fullStr | Analysis of the Epitope Structure of Plum pox virus Coat Protein |
| title_full_unstemmed | Analysis of the Epitope Structure of Plum pox virus Coat Protein |
| title_short | Analysis of the Epitope Structure of Plum pox virus Coat Protein |
| title_sort | analysis of the epitope structure of plum pox virus coat protein |
| url | http://hdl.handle.net/20.500.11939/4947 |
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