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

نویسندگان

  • Stanislav V. Sosnovtsev
  • Svetlana A. Sosnovtseva
  • STANISLAV V. SOSNOVTSEV
  • SVETLANA A. SOSNOVTSEVA
چکیده

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Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase.

Feline calicivirus (FCV), a member of the Caliciviridae, 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 th...

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Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genome.

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Feline calicivirus capsid protein expression and capsid assembly in cultured feline cells.

The capsid protein of feline calicivirus (FCV) was expressed by using plasmids containing cytomegalovirus, simian virus 40, or T7 promoters. The strongest expression was achieved with the T7 promoter and coinfection with vaccinia virus expressing the T7 RNA polymerase (MVA/T7pol). The FCV precursor capsid protein was processed to the mature-size protein, and these proteins were assembled in to ...

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A Proposal for a Structural Model of the Feline Calicivirus Protease Bound to the Substrate Peptide under Physiological Conditions

Feline calicivirus (FCV) protease functions to cleave viral precursor proteins during productive infection. Previous studies have mapped a protease-coding region and six cleavage sites in viral precursor proteins. However, how the FCV protease interacts with its substrates remains unknown. To gain insights into the interactions, we constructed a molecular model of the FCV protease bound with th...

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تاریخ انتشار 1998