| Literature DB >> 567468 |
Abstract
Hog cholera virus grown in PK-15 cells was purified by centrifugation through a sucrose cushion followed by sucrose gradient centrifugation. Analysis of virus labeled externally with [3H]sodium borohydride on polyacrylamide gel electrophoresis revealed two glycoproteins, gp55 and gp46. A third structural polypeptide, p36, seems not to be glycosylated. The gp46 was also found in the virus-free supernatant of infected cells. It could be demonstrated by radioimmune precipitation of virus labeled with[35S]methionine that all three polypeptides are specific for hog cholera virions. Electron microscopically hog cholera virus appeared as a spherical particle with a diameter of 42 +/- 8 nm. The virus particles frequently displayed a fringe of projections with a length of about 6--8 nm. The similarities of hog cholera virus with Alphaviruses and Flaviviruses are discussed.Entities:
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Year: 1978 PMID: 567468 DOI: 10.1007/bf01320073
Source DB: PubMed Journal: Arch Virol ISSN: 0304-8608 Impact factor: 2.574