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SummaryParticles of the Puerto Rico isolate of cowpea mosaic virus (CPMV-PR), which belongs in the severe subgroup, had one electrophoretic form when analysed by 2.5% polyacrylamide gel electrophoresis and zone electrophoresis in sucrose gradients at pH 7.8, 7.5, and 5.5. The electrophoretic properties of CPMV-PR did not vary with time after inoculation but the virus could be converted to a slower migrating form by in vitro treatment with trypsin. The partial conversion by trypsin was accompanied by and was possibly the result of proteolytic conversion of the S protein subunit to a lower molecular mass form. Analysis of proteins of untreated CPMV-PR suggested that the S subunit of the virus could also be converted in vivo by plant proteases to a smaller form without any change in the particle net surface charge, while in vitro treatment with trypsin affected those S subunits not previously converted by plant proteases, by converting them to a form slightly larger and with a greater positive charge than the S subunit produced by action of the plant proteases. This hypothesis accounts both for the decrease in electrophoretic mobility and for the fact that the conversion was only partial.

Electrophoretic Properties of Cowpea Mosaic Virus (Severe Subgroup)