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1 CNRS-UPR 2511, IBL/Institut Pasteur de Lille, 59021 Lille Cedex, France
2 Laboratoire de Virologie, Centre Hospitalier Universitaire-Hôpital Sud, 80054 Amiens Cedex, France
3 CERVI (Virologie), UPRES EA 2387, Hôpital Pitié-Salpêtrière, 75651 Paris Cedex 13, France
Correspondence
Czeslaw Wychowski
czeslaw.wychowski{at}ibl.fr
Hepatitis C virus (HCV) is an important human pathogen that affects 170 million people worldwide. The HCV genome is approximately 9·6 kb in length and encodes a polyprotein that is proteolytically cleaved to generate at least 10 mature viral protein products. Recently, a new protein, named F, has been described to be expressed through a ribosomal frameshift within the capsid-encoding sequence, a mechanism unique among members of the family Flaviviridae. Here, expression of the F protein was investigated in an in vitro transcription/translation assay. Its expression in mammalian cells was confirmed using specific recombinant vaccinia viruses; under these conditions, protein expression is dependent on the HCV IRES. The F protein was tagged with firefly luciferase or the Myc epitope to facilitate its identification. Ribosomal frameshifting was dependent on the presence of mutations in the capsid-encoding sequence. No frameshifting was detected in the absence of any mutation. Furthermore, analysis of the F protein in time-course experiments revealed that the protein is very unstable and that its production can be stabilized by the proteasome inhibitor MG132. Finally, indirect immunofluorescence studies have localized the F protein in the cytoplasm, with notable perinuclear detection.
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