Abstract
Virions of bovine papilloma virus (BPV) were isolated from a pool of cutaneous bovine fibropapillomas and purified by CsCl gradient centrifugation. SDS-PAGE revealed several polypeptides with an Mr ranging from 76K to 19K. Western blot analysis of the viral isolate identified additional polypeptides when a rabbit anti-BPV serum was used, but only the main capsid component of 57K when a rabbit antiserum raised against human papillomavirus was used. The viral preparation was then 125I-labelled and further purified by gel filtration. SDS-PAGE of immunoprecipitates of the anti-BPV serum with different fractions from the chromatographic column revealed the polypeptides of 76K, 57K and 28K to be viral structural components. The 28K polypeptide, not previously characterized, was shown to be composed of several molecular forms, migrating over a pH range of 3.5 to 4.6 when analysed by two-dimensional PAGE. Following SDS-PAGE performed under non-reducing conditions, the 28K and 76K polypeptides and the main capsid component of 57K appeared to be linked by disulphide bridges to form hetero- or homopolymers.
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