Comparison of Molecular and Growth Properties for Two Different Canine Distemper Virus Clusters, Asia 1 and 2, in Japan

Abstract

ABSTRACT. To compare the molecular and growth properties of two newly isolated canine distemper virus strains in the Asia 1 and 2 groups with clinico-pathological findings in dogs, nucleotide and predicted amino acid sequence comparisons of genes H and P were performed together with comparative growth profiling. The predicted amino acid sequences of the H gene contained 12 cysteine residues that were conserved among the examined Asia 1 and Asia 2 viruses. The hydrophobic region in the H gene of the Asia 2 isolates was one amino acid longer than that of the Asia 1 group. The H gene of the Asia 1 group had nine putative asparagine (N)-linked glycosylation sites, while there were eight sites in the Asia 2 group. The titers of the cell-associated viruses for the Asia 1 strains were higher than those of the released viruses and were opposite to those of the Asia 2 strains in a previous study. The molecular and growth properties of the Asia 1 and Asia 2 groups seem to vary, although no significant differences were observed in the clinical signs and pathological findings between the two groups.

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Identification of a new genotype of canine distemper virus circulating in America

“…It has been described that changes in N-glycosylation of the H protein may affect neutralization by antibodies and replication in vitro (Harder et al 1996;Iwatsuki et al 1997;Lan et al 2007). On the basis of the partial H protein fragment, the Mexican strains differed from the vaccine strain Ondesterpoort, since they retained N-glycosylation potential sites that are conserved in the majority of field CDVs and that are missing in strain Ondesterpoort.…”

Molecular characteristics of a canine distemper virus isolated from mink (Neovison vison) in Shandong, China, 2013

“…Differences in n-linked glycosylation of the H protein may result in differences in neutralization efficacy, replication and virulence of CDV (15)(16). The n-linked glycosylation site 309-311 is generally specific to field isolates but not to vaccine strains (17), and therefore is possibly relevant to CDV virulence.…”