Sequence analysis and expression of the attachment and fusion proteins of canine distemper virus wild-type strain A75/17.

ABSTRACT: The biological properties of wild-type A75/17 and cell culture-adapted Onderstepoort canine distemper virus differ markedly. To learn more about the molecular basis for these differences, we have isolated and sequenced the protein-coding regions of the attachment and fusion proteins of wild-type canine distemper virus strain A75/17. In the attachment protein, a total of 57 amino acid differences were observed between the Onderstepoort strain and strain A75/17, and these were distributed evenly over the entire protein. Interestingly, the attachment protein of strain A75/17 contained an extension of three amino acids at the C terminus. Expression studies showed that the attachment protein of strain A75/17 had a higher apparent molecular mass than the attachment protein of the Onderstepoort s

SUBMITTER: Cherpillod P 

PROVIDER: S-EPMC104471 | biostudies-literature | 1999 Mar

REPOSITORIES: biostudies-literature