Porcine parvovirus (PPV) was extensively purified from infected swine fetal homogenates by CaCl2 precipitation followed by CsCl density centrifugation. Two species of particles possessing PPV-specific hemagglutinating activity were observed banding at densities of 1.39 and 1.30 g/ml, representing full and empty 20-nm virion particles, respectively. Both classes of particles contained three major polypeptides, A, B, and C, with respective molecular weights of 83,000, 64,000, and 60,000. The amount of polypeptide A was similar in both species (approximately 10%); however, the B protein was most abundant in the 1.30-g/ml particles, whereas the C protein was the major polypeptide found in the 1.39-g/ml particles. Antisera generated to each sodium dodecyl sulfate-polyacrylamide gel-purified virion structural protein had reactivities qualitatively similar to those of conventional antisera raised against intact PPV in a variety of standard serological assays. The antisera generated against the individual sodium dodecyl sulfate-denatured PPV polypeptides were able to react with native, intact PPV virions and were capable of neutralizing virus infectivity.
|Original language||English (US)|
|Number of pages||13|
|Journal||Journal of virology|
|State||Published - Jan 1 1983|