Heterogeneity in the capsid protein of bovine enteric caliciviruses belonging to a new genus

• Published in: Virology (New York, N.Y.) Vol. 387; no. 1; pp. 109 - 116
• Main Authors: D'Mello, Felicity, Jervis, Sarah M, Edwards, Paul M, Oliver, Stefan L, Bridger, Janice C
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 25.04.2009
• Subjects: Amino Acid Sequence; amino acid sequences; Animals; antigenic variation; Bayesian theory; Bovine; bovine enteric caliciviruses; Caliciviridae; Caliciviridae - chemistry; Caliciviridae - classification; Caliciviridae - genetics; Calicivirus; Capsid - chemistry; Capsid Proteins - chemistry; Capsid Proteins - genetics; Capsid sequence heterogeneity; Cattle; cattle diseases; coat proteins; diarrhea; Enteric; Feces - virology; Genetic Variation; Infectious Disease; Models, Molecular; Molecular Sequence Data; Norovirus; Phylogeny; Protein Structure, Tertiary; provenance; RNA, Viral - genetics; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; viral antigens; viral enteritis; United Kingdom; South Korea; United States; Japan; Capsid sequence heterogeneity; Calicivirus; Bovine; Enteric
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1016/j.virol.2009.01.035

Abstract Some bovine enteric caliciviruses form a new genus in the family Caliciviridae . In this study, Bayesian phylogenetic analysis of 31 full length capsid sequences from Europe, North America and Asia revealed that this new genus had four currently circulating lineages that showed both temporal and geographical distribution. These groupings were supported by the distribution of the frequency of pair-wise distances. However, the nucleotide and amino acid heterogeneity was low, with a maximum nucleotide and amino acid divergence of 16.7% and 8.4%, respectively. Most variability was found between amino acid residues 288 and 420 of the capsid protein and the sequence motifs observed in this region supported the division of the four lineages. Homology modelling using the structure of the San Miguel sea lion capsid indicated that most variation occurred in the predicted P2 domain and thus, may affect antigenic sites on the surface of the capsid of this newly described genus.