1997
DOI: 10.1099/0022-1317-78-2-373
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Molecular and phylogenetic analyses of the haemagglutinin (H) proteins of field isolates of canine distemper virus from naturally infected dogs.

Abstract: We isolated three strains of canine distemper virus (CDV) -the Ueno, Hamamatsu, and Yanaka strains -from dogs in Japan and analysed the molecular properties of their haemagglutinin (H) proteins. Immunoprecipitation of all three strains with a monoclonal antibody revealed H proteins with molecular masses of 84 kDa, which differs from the molecular mass (78 kDa) of the H protein of the Onderstepoort vaccine strain. However, after tunicamycin treatment immunoprecipitation identified H proteins of identical molecu… Show more

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Cited by 100 publications
(104 citation statements)
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“…The genetic relationship was closer between the recent field isolates, the Yanaka strain and PDV-2, than between the Yanaka and Onderstepoort vaccine strains. These data were in agreement with the result from the H genes [14], and suggest a progressive evolution in wild-type CDV isolates. The significant alteration of PDV-2 F gene was noted as the lack of the third ATG triplet at positions nt 461 to 463 [28], which is selectively required for in vitro translation of the Onderstepoort F gene [6].…”
supporting
confidence: 90%
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“…The genetic relationship was closer between the recent field isolates, the Yanaka strain and PDV-2, than between the Yanaka and Onderstepoort vaccine strains. These data were in agreement with the result from the H genes [14], and suggest a progressive evolution in wild-type CDV isolates. The significant alteration of PDV-2 F gene was noted as the lack of the third ATG triplet at positions nt 461 to 463 [28], which is selectively required for in vitro translation of the Onderstepoort F gene [6].…”
supporting
confidence: 90%
“…4) in contrast to the finding that the glycosylation properties of the H proteins varied between the isolates and the vaccine strains [14]. The similar molecular sizes revealed by the immunoprecipitation analysis may provide the evidence of the same glycosylation properties of these F proteins.…”
mentioning
confidence: 87%
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