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Analysis of the Epitope Structure of Plum pox virus Coat Protein

hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorCANDRESSE, Thierry
hal.structure.identifierConsejo Superior de Investigaciones Cientificas [España] = Spanish National Research Council [Spain] [CSIC]
dc.contributor.authorSAENZ, Pilar
hal.structure.identifierConsejo Superior de Investigaciones Cientificas [España] = Spanish National Research Council [Spain] [CSIC]
dc.contributor.authorGARCÍA, Juan Antonio
hal.structure.identifierIstituto di Virologia Vegetale
dc.contributor.authorBOSCIA, Donato
hal.structure.identifierPalacky University Olomouc
dc.contributor.authorNAVRATIL, Milan
hal.structure.identifierInstituto Valenciano de Investigaciones Agrarias - Institut Valencià d'Investigacions Agraries - Valencian Institute for agricultural Research [IVIA]
dc.contributor.authorGORRIS, Maria Teresa
hal.structure.identifierInstituto Valenciano de Investigaciones Agrarias - Institut Valencià d'Investigacions Agraries - Valencian Institute for agricultural Research [IVIA]
dc.contributor.authorCAMBRA, Mariano
dc.date.issued2011
dc.identifier.issn0031-949X
dc.description.abstractEnTyping 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.isoen
dc.publisherAmerican Phytopathological Society
dc.title.enAnalysis of the Epitope Structure of Plum pox virus Coat Protein
dc.typeArticle de revue
dc.identifier.doi10.1094/PHYTO-10-10-0274
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie
bordeaux.journalPhytopathology
bordeaux.page611-619
bordeaux.volume101
bordeaux.issue5
bordeaux.peerReviewedoui
hal.identifierhal-02646785
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02646785v1
bordeaux.COinSctx_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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