Analysis of the Epitope Structure of Plum pox virus Coat Protein
hal.structure.identifier | Biologie du fruit et pathologie [BFP] | |
dc.contributor.author | CANDRESSE, Thierry | |
hal.structure.identifier | Consejo Superior de Investigaciones Cientificas [España] = Spanish National Research Council [Spain] [CSIC] | |
dc.contributor.author | SAENZ, Pilar | |
hal.structure.identifier | Consejo Superior de Investigaciones Cientificas [España] = Spanish National Research Council [Spain] [CSIC] | |
dc.contributor.author | GARCÍA, Juan Antonio | |
hal.structure.identifier | Istituto di Virologia Vegetale | |
dc.contributor.author | BOSCIA, Donato | |
hal.structure.identifier | Palacky University Olomouc | |
dc.contributor.author | NAVRATIL, Milan | |
hal.structure.identifier | Instituto Valenciano de Investigaciones Agrarias - Institut Valencià d'Investigacions Agraries - Valencian Institute for agricultural Research [IVIA] | |
dc.contributor.author | GORRIS, Maria Teresa | |
hal.structure.identifier | Instituto Valenciano de Investigaciones Agrarias - Institut Valencià d'Investigacions Agraries - Valencian Institute for agricultural Research [IVIA] | |
dc.contributor.author | CAMBRA, Mariano | |
dc.date.issued | 2011 | |
dc.identifier.issn | 0031-949X | |
dc.description.abstractEn | 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-IVIA 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. | |
dc.language.iso | en | |
dc.publisher | American Phytopathological Society | |
dc.title.en | Analysis of the Epitope Structure of Plum pox virus Coat Protein | |
dc.type | Article de revue | |
dc.identifier.doi | 10.1094/PHYTO-10-10-0274 | |
dc.subject.hal | Sciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie | |
bordeaux.journal | Phytopathology | |
bordeaux.page | 611-619 | |
bordeaux.volume | 101 | |
bordeaux.issue | 5 | |
bordeaux.peerReviewed | oui | |
hal.identifier | hal-02646785 | |
hal.version | 1 | |
hal.popular | non | |
hal.audience | Internationale | |
hal.origin.link | https://hal.archives-ouvertes.fr//hal-02646785v1 | |
bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Phytopathology&rft.date=2011&rft.volume=101&rft.issue=5&rft.spage=611-619&rft.epage=611-619&rft.eissn=0031-949X&rft.issn=0031-949X&rft.au=CANDRESSE,%20Thierry&SAENZ,%20Pilar&GARC%C3%8DA,%20Juan%20Antonio&BOSCIA,%20Donato&NAVRATIL,%20Milan&rft.genre=article |
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