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Molecular characterization of morphologically typical human calicivirus Sapporo

Numata, K., Hardy, M. E., Nakata, S., Chiba, S., Estes, M. K.
Archives of virology 1997 v.142 no.8 pp. 1537-1552
DNA-directed RNA polymerase, Norwalk virus, Rabbit hemorrhagic disease virus, Sapporo virus, amino acids, capsid, children, complementary DNA, gastroenteritis, genome, open reading frames, proteins, sequence analysis, virus-like particles, viruses
Human calicivirus Sapporo (SV) has typical calicivirus morphology and causes acute gastroenteritis in children. The nucleotide sequence of 3.2 kb of the 3′ end of SV was determined from a cloned cDNA. The 3′ end of the SV genome is predicted to encode the RNA-dependent RNA polymerase region, the capsid protein and two small open reading frames. The nonstructural and capsid protein coding sequences in the SV genome are fused in a single open reading frame. The organization of these proteins in the SV sequence is similar to that of rabbit hemorrhagic disease virus and the recently described Manchester virus, and distinct from the genome organization of the prototype human calicivirus, Norwalk virus, that lacks typical calicivirus morphology and has been described as a small round structured virus (SRSV). Sequence analysis of the predicted capsid region showed that the SV capsid is longer by ∼30 amino acids than the capsid of any of the SRSVs, and multiple sequence alignments showed that these additional amino acids are located in the variable region of the capsid protein. Expression of the capsid protein of SV in insect cells resulted in the self-assembly of virus-like particles that have a morphology similar to that of the native virus. This result shows that calicivirus morphology is determined by the primary sequence of the capsid protein.