Fusion protein gene nucleotide sequence similarities, shared antigenic sites and phylogenetic analysis suggest that phocid distemper virus type 2 and canine distemper virus belong to the same virus entity

• Published in: Journal of general virology 1993-09, Vol.74 (9), p.1989-1994
• Main Authors: Visser, Ilona K. G, van der Heijden, Roger W. J, van de Bildt, Marco W. G, Kenter, Marcel J. H, Orvell, Claes, Osterhaus, Albert D. M. E
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; canine distemper virus; Codon - genetics; Distemper Virus, Canine - genetics; DNA, Viral - genetics; Fundamental and applied biological sciences. Psychology; Genes, Viral; Genetics; Measles virus - genetics; Microbiology; Molecular Sequence Data; Molecular Weight; Paramyxoviridae - genetics; Paramyxoviridae - isolation & purification; Phylogeny; RNA, Messenger - genetics; Seals, Earless; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Viral Fusion Proteins - biosynthesis; Viral Fusion Proteins - genetics; Viral Fusion Proteins - isolation & purification; Virology
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-74-9-1989

1 Seal Rehabilitation and Research Centre, Hoofdstraat 94a, 9968 AG Pieterburen 2 Laboratory of Immunobiology, National Institute of Public Health and Environmental Protection, P.O. Box 1, 3720 BA Bilthoven and 3 Division of Virology, Department of Infectious Diseases and Immunology, Veterinary Faculty, State University of Utrecht, Yalelaan 1, 3508 TD Utrecht, The Netherlands and 4 Central Microbiological Laboratory of Stockholm City Council, Department of Virology, S-107-26 Stockholm, Sweden Nucleotide sequencing of the fusion protein (F) gene of phocid distemper virus-2 (PDV-2), recently isolated from Baikal seals ( Phoca sibirica ), revealed an open reading frame (nucleotides 84 to 2075) with two potential in-frame ATG translation initiation codons. We suggest that the second in-frame ATG triplet at positions 264 to 266 initiates the translation, resulting in a protein of 537 amino acid residues with a calculated M r of 63035. The putative F1/F2 cleavage site, located approximately 100 amino acid residues from the N terminus, is identical to those of the F proteins of phocid distemper virus-1 (PDV-1) isolated from European harbour seals ( Phoca vitulina ) and of canine distemper virus (CDV). A full scale comparison of morbillivirus F genes reveals that the conserved F0 extracellular protein-encoding region contains a large number of non-expressed mutations, suggesting that this part of the protein is under strong functional constraints. Phylogenetic analysis of morbillivirus F gene nucleotide sequences revealed a closer evolutionary relationship between PDV-2 and CDV than between PDV-1 and PDV-2. These data were supported by cross-reactivity patterns of PDV-2 and CDV obtained with monoclonal antibodies to structural proteins of PDV-1 and CDV, and suggest that PDV-2 is a strain of CDV, resulting from a trans-species infection. Received 10 March 1993; accepted 13 May 1993.