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Mapping and structural analysis of B-cell epitopes on the morbillivirus nucleoprotein amino terminus

¹ Animal Production Unit, FAO/AIEA Agriculture and Biotechnology Laboratory, IAEA Laboratories, A-2444 Seibersdorf, Austria
² CIRAD-Département EMVT, UPR ‘Contrôle des maladies animales et exotiques’, TA/30G, Campus International de Baillarguet, F-34398 Montpellier Cedex 5, France

Correspondence
G. Libeau
genevieve.libeau{at}cirad.fr

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.

The GenBank/EMBL/DDBJ accession numbers for the sequences described in this study are EF186057–EF186059.