Archives of Virology

, Volume 66, Issue 3, pp 193–206 | Cite as

Structural polypeptides of canine distemper virus

  • C. Örvell
Original Papers

Summary

The structural polypeptides of two strains of canine distemper virus and the Lec strain of measles virus were analysed by SDS-polyacrylamide-slab-gel electrophoresis. One strain of canine distemper virus derived from a live vaccine (Convac, Dumex), contained six major structural polypeptides with mol. wt. of 85, 78, 59, 43, 41 and 34×103. The 85K polypeptide was glycosylated. It was interpreted to be equivalent to the 79K glycoprotein of the measles hemagglutinin.

The second strain, a rapidly growing variant of the Onderstepoort strain of canine distemper virus characterized by extensive syncytium forming cytopathic effects in tissue culture, contained the 59, 43, 41 and 34K polypeptides, but the 85 and 78K polypeptides were not present in detectable amounts. The 43K polypeptide was identified as cellular actin by limited proteolysis. By use of monospecific rabbit hyperimmune sera against each of the major structural polypeptides of measles virus, the 59, 41 and 34K structural polypeptides could be identified as nucleocapsid protein (NP), fusion (F) polypeptide, and the membrane (M) polypeptide, respectively. In neutralization tests with rabbit hyperimmune sera against each of the two strains, this Onderstepoort strain, which contained reduced amounts of the hemagglutinin glycoprotein, gave higher neutralization titers than the vaccine strain.

Keywords

Polypeptide Measle Vaccine Strain Measle Virus Neutralization Test 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1980

Authors and Affiliations

  • C. Örvell
    • 1
  1. 1.Department of VirologyKarolinska Institutet, School of MedicineStockholmSweden

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