Porcine parvovirus: virus purification and structural and antigenic properties of virion polypeptides

T. W. Molitor, H. S. Joo, M. S. Collett

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)842-854
Number of pages13
JournalJournal of virology
Volume45
Issue number2
StatePublished - Jan 1 1983

Fingerprint

Dive into the research topics of 'Porcine parvovirus: virus purification and structural and antigenic properties of virion polypeptides'. Together they form a unique fingerprint.

Cite this