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REPLICATION

Isolation of Enzymatically Active Replication Complexes from Feline Calicivirus-Infected Cells

Kim Y. Green, Aaron Mory, Mark H. Fogg, Andrea Weisberg, Gaël Belliot, Mariam Wagner, Tanaji Mitra, Ellie Ehrenfeld, Craig E. Cameron, Stanislav V. Sosnovtsev
Kim Y. Green
1National Institutes of Health, Bethesda, Maryland
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  • For correspondence: kgreen@niaid.nih.gov
Aaron Mory
2Pennsylvania State University, University Park, Pennsylvania
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Mark H. Fogg
1National Institutes of Health, Bethesda, Maryland
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Andrea Weisberg
1National Institutes of Health, Bethesda, Maryland
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Gaël Belliot
1National Institutes of Health, Bethesda, Maryland
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Mariam Wagner
1National Institutes of Health, Bethesda, Maryland
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Tanaji Mitra
1National Institutes of Health, Bethesda, Maryland
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Ellie Ehrenfeld
1National Institutes of Health, Bethesda, Maryland
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Craig E. Cameron
2Pennsylvania State University, University Park, Pennsylvania
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Stanislav V. Sosnovtsev
1National Institutes of Health, Bethesda, Maryland
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DOI: 10.1128/JVI.76.17.8582-8595.2002
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ABSTRACT

A membranous fraction that could synthesize viral RNA in vitro in the presence of magnesium salt, ribonucleotides, and an ATP-regenerating system was isolated from feline calicivirus (FCV)-infected cells. The enzymatically active component of this fraction was designated FCV replication complexes (RCs), by analogy to other positive-strand RNA viruses. The newly synthesized RNA was characterized by Northern blot analysis, which demonstrated the production of both full-length (8.0-kb) and subgenomic-length (2.5-kb) RNA molecules similar to those synthesized in FCV-infected cells. The identity of the viral proteins associated with the fraction was investigated. The 60-kDa VP1 major capsid protein was the most abundant viral protein detected. VP2, a minor structural protein encoded by open reading frame 3 (ORF3), was also present. Nonstructural proteins associated with the fraction included the precursor polypeptides Pro-Pol (76 kDa) and p30-VPg (43 kDa), as well as the mature nonstructural proteins p32 (derived from the N-terminal region of the ORF1 polyprotein), p30 (the putative “3A-like” protein), and p39 (the putative nucleoside triphosphatase). The isolation of enzymatically active RCs containing both viral and cellular proteins should facilitate efforts to dissect the contributions of the virus and the host to FCV RNA replication.

  • Copyright © 2002 American Society for Microbiology
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Isolation of Enzymatically Active Replication Complexes from Feline Calicivirus-Infected Cells
Kim Y. Green, Aaron Mory, Mark H. Fogg, Andrea Weisberg, Gaël Belliot, Mariam Wagner, Tanaji Mitra, Ellie Ehrenfeld, Craig E. Cameron, Stanislav V. Sosnovtsev
Journal of Virology Sep 2002, 76 (17) 8582-8595; DOI: 10.1128/JVI.76.17.8582-8595.2002

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Isolation of Enzymatically Active Replication Complexes from Feline Calicivirus-Infected Cells
Kim Y. Green, Aaron Mory, Mark H. Fogg, Andrea Weisberg, Gaël Belliot, Mariam Wagner, Tanaji Mitra, Ellie Ehrenfeld, Craig E. Cameron, Stanislav V. Sosnovtsev
Journal of Virology Sep 2002, 76 (17) 8582-8595; DOI: 10.1128/JVI.76.17.8582-8595.2002
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KEYWORDS

Calicivirus, Feline
Cell Membrane
RNA, Viral
Viral Proteins
virus replication

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