Mapping and structural analysis of B-cell epitopes on the morbillivirus nucleoprotein amino terminus
By analysing the antigenic structure of the morbillivirus nucleoprotein (N) using a competitive-binding assay of monoclonal antibodies (mAbs), six different antigenic sites were identified previously. By using Pepscan methodology complemented by analysis of truncated N proteins, a better characterization of five of these antigenic sites was provided: I, II, III, IV and VI. mAbs specific to Rinderpest virus, defining antigenic sites II, III and IV, and those common to four morbilliviruses, delineating sites I and VI, were analysed in the present study. It was found that all but one mapped to the same region, between aa 120 and 149 of N. However, the mAb 3-1 epitope was located in the carboxy-terminal region (aa 421-525). This result may indicate the high immunogenicity of the amino-terminal variable region, at least in the mouse. It was surprising that the epitope of mAb 33-4, antigenic site VI, which recognized all morbilliviruses so far tested, was located in one of the two non-conserved regions between morbillivirus N proteins. It is shown that the conserved amino acid motif 126EAD128----131F-------148EN149 is critical for epitope constitution and recognition.
| Main Authors: | , , , , |
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| Format: | article biblioteca |
| Language: | eng |
| Published: |
The Microbiology Society
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| Subjects: | L73 - Maladies des animaux, |
| Online Access: | http://agritrop.cirad.fr/537516/ http://agritrop.cirad.fr/537516/1/537516.pdf |
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