Abstract
Highly specific monoclonal antibodies raised against virus-like particles (VLPs) from male sterile Vicia faba were purified and conjugated to glutaraldehyde-activated sepharose. This matrix was then used for VLP purification by affinity chromatography and the presence of VLPs in the eluate was checked by a quantitative and highly sensitive ELISA. No protein could be detected in the purified VLP fractions. Comparative chemical and enzymatic treatments performed on purified VLPs indicated that the epitope recognized by the monoclonal antibodies was resistant to protease digestion, was mostly hydrophilic and was degraded by a specific treatment to glycosidic components. Thus, this epitope contains sugars.
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