CANDRESSE, Thierry; SAENZ, Pilar; GARCÍA, Juan Antonio; BOSCIA, Donato; NAVRATIL, Milan; GORRIS, Maria Teresa; CAMBRA, Mariano

doi:10.1094/PHYTO-10-10-0274

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CANDRESSE, Thierry
Biologie du fruit et pathologie [BFP]

SAENZ, Pilar
Consejo Superior de Investigaciones Cientificas [España] = Spanish National Research Council [Spain] [CSIC]

GARCÍA, Juan Antonio
Consejo Superior de Investigaciones Cientificas [España] = Spanish National Research Council [Spain] [CSIC]

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Phytopathology. 2011, vol. 101, n° 5, p. 611-619

American Phytopathological Society

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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.< Réduire

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Analysis of the Epitope Structure of Plum pox virus Coat Protein

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