Publication Date:
2002
abstract:
Previously characterized monoclonal antibodies (MAbs) to Grapevine
virus A (GVA) showed a differential reactivity against intact or partially
destabilized virus particles [2]. In the present study, this differential
reactivity was confirmed and several peptides reacting with a panel
of four different antibodies were identified by the PEPSCAN method of
epitope mapping. Oligopeptide sequences comprised between coat
protein residues 61 (V) and 72 (T) were recognized by all the
antibodies tested. One of these peptides (VGPKASK) was also
reactive when expressed on recombinant phage particles as a fusion
protein with protein pVIII. The specificity of this sequence for
antibody binding was also demonstrated by competitive-ELISA using
one of the GVA MAbs. The results of this study suggest that GVA
particles carry a highly structured epitope centered on a common
peptide region of the coat protein sequence.
virus A (GVA) showed a differential reactivity against intact or partially
destabilized virus particles [2]. In the present study, this differential
reactivity was confirmed and several peptides reacting with a panel
of four different antibodies were identified by the PEPSCAN method of
epitope mapping. Oligopeptide sequences comprised between coat
protein residues 61 (V) and 72 (T) were recognized by all the
antibodies tested. One of these peptides (VGPKASK) was also
reactive when expressed on recombinant phage particles as a fusion
protein with protein pVIII. The specificity of this sequence for
antibody binding was also demonstrated by competitive-ELISA using
one of the GVA MAbs. The results of this study suggest that GVA
particles carry a highly structured epitope centered on a common
peptide region of the coat protein sequence.
Iris type:
01.01 Articolo in rivista
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