PURIFICATION BY MONOCLONAL-ANTIBODY AFFINITY-CHROMATOGRAPHY OF VIRUS-LIKE PARTICLES ASSOCIATED WITH THE 447 CYTOPLASMIC MALE-STERILITY OF VICIA-FABA AND INVESTIGATION OF THEIR ANTIGENIC COMPOSITION

Highly specific monoclonal antibodies raised against virus-like partic les (VLPs) from male sterile Vicia faba were purified and conjugated t o glutaraldehyde-activated sepharose. This matrix was then used for VL P purification by affinity chromatography and the presence of VLPs in the eluate was checked by a quantitative and highly sensitive ELISA. N o protein could be detected in the purified VLP fractions. Comparative chemical and enzymatic treatments performed on purified VLPs indicate d that the epitope recognized by the monoclonal antibodies was resista nt to protease digestion, was mostly hydrophilic and was degraded by a specific treatment to glycosidic components. Thus, this epitope conta ins sugars.