Purification of Soybean Mosaic Virus by Affinity Chromatography Using Monoclonal Antibodies

Abstract

Immunoaffinity columns were prepared by covalently binding monoclonal antibodies specific for soybean mosaic virus (SMV) to an agarose support matrix. SMV, purified by binding and elution, contained no contaminating proteins detectable by SDS-polyacrylamide gel electrophoresis. Affinity-purified SMV was essentially identical to virus purified by standard procedures in its infectivity, u.v. absorbance spectrum ratio of A280/A260, sedimentation coefficient, electrophoretic pattern of coat protein, morphology and antigenicity. This method of purification is rapid, reproducible, and yields highly purified virus preparations. It may therefore be applicable in the purification of a wide variety of plant viruses.