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Antigenic analysis of the coat protein of beet necrotic yellow vein virus by means of monoclonal antibodies

L. Torrance^2,

¹ Biologische Bundesanstalt für Land- und Forstwirtschaft, Institute für Viruskrankheiten der Pflanzen und Biochemie, Messeweg 11, D-3300 Braunschweig, F.R.G.
² MAFF Harpenden Laboratory, Hatching Green, Harpenden, Hertfordshire AL5 2BD, U.K.
³ Istituto Sperimentale per le Colture Industriali, S.O.P. di Rovigo, I-45100 Rovigo, Italy
⁴ Laboratoire de Biologie Cellulaire et Moléculaire, F-63170 Aubiere, France
and⁵ Laboratory for Monoclonal Antibodies, NL-6700 GW Wageningen, The Netherlands

By means of monoclonal antibodies (MAbs), five (groups of) epitopes were identified on particles of beet necrotic yellow vein virus (BNYVV). Epitopes 1 and 2, which were located on the opposite extremities of virus particles, are discontinuous (SDS-labile) epitopes which were destroyed when the particles were treated with trypsin. Epitope 3 is a continuous (SDS-stable) epitope lcoated at the same extremity as epitope 2. It was not destroyed when the particles were treated with trypsin and was present on an Escherichia coli-expressed fusion protein containing amino acids (aa) 1 to 103 of the BNYVV coat protein. The continuous epitope 4, which was located along the entire length of the particles, was found to be present on a fusion protein containing aa 104 to 188 of the BNYVV coat protein but not on trypsin-treated virus particles. In Western blots, these treated particles yielded two slightly smaller coat proteins which failed to react with MAbs specific for epitope 4 but did react with polyclonal antisera and MAbs specific for epitope 3. BNYVV coat protein has a trypsin cleavage site on the carboxyl side of arginine in position 182, so it is therefore suggested that epitope 4 is located on the exposed C terminus, which is composed of aa 183 to 188. Epitope 5 was also located along the entire length of the particles but in a more uneven distribution than epitope 4. This may be because it is a discontinuous epitope that is very sensitive to subtle changes in protein conformation.

Present address: Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, U.K.

Received 2 April 1990; accepted 11 June 1990.