Cleavage of the Feline Calicivirus Capsid Precursor Is Mediated by a Virus-Encoded Proteinase

@article{Sosnovtsev1998CleavageOT,
  title={Cleavage of the Feline Calicivirus Capsid Precursor Is Mediated by a Virus-Encoded Proteinase},
  author={S. Sosnovtsev and S. Sosnovtseva and K. Green},
  journal={Journal of Virology},
  year={1998},
  volume={72},
  pages={3051 - 3059}
}
ABSTRACT Feline calicivirus (FCV), a member of theCaliciviridae, produces its major structural protein as a precursor polyprotein from a subgenomic-sized mRNA. In this study, we show that the proteinase responsible for processing this precursor into the mature capsid protein is encoded by the viral genome at the 3′-terminal portion of open reading frame 1 (ORF1). Protein expression studies of either the entire or partial ORF1 indicate that the proteinase is active when expressed either in in… Expand
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An entire open reading frame in a cDNA encoding the capsid protein gene of feline calicivirus was subcloned into a mammalian expression vector and suggested that three neutralizing epitopes had a conformational nature and that the other four linear epitopes were related to 74 amino acid residues between positions 381 and 454 in the protein, in which high variation was known to be present among three strains of FCV. Expand
Antigenic analysis of feline calicivirus capsid precursor protein and its deleted polypeptides produced in a mammalian cDNA expression system
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An entire open reading frame in a cDNA encoding the capsid protein gene of feline calicivirus was subcloned into a mammalian expression vector and suggested that three neutralizing epitopes had a conformational nature and that the other four linear epitopes were related to 74 amino acid residues between positions 381 and 454 in the protein, in which high variation was known to be present among three strains of FCV. Expand
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