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Hepatitis C virus p7: molecular function and importance in hepatitis C virus life cycle and potential antiviral target
Author(s) -
Khaliq Saba,
Jahan Shah,
Hassan Sajida
Publication year - 2011
Publication title -
liver international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.873
H-Index - 110
eISSN - 1478-3231
pISSN - 1478-3223
DOI - 10.1111/j.1478-3231.2010.02442.x
Subject(s) - hepatitis c virus , virology , virus , transmembrane protein , viral life cycle , biology , ion channel , in vitro , ns2 3 protease , biochemistry , viral replication , receptor
p7, a 63‐residue peptide encoded by hepatitis C virus (HCV), a major pathogen associated with a risk of developing severe liver disease, is involved in ion channel activity in lipid bilayer membranes both in in vitro and cell‐based assays. p7 protein consists of two transmembrane α‐helices, TM1 and TM2 connected by a loop oriented towards the cytoplasm. HCV relies on p7 function in addition to ion channel formation for efficient assembly, release and production of infectious progeny virions from liver cells. p7 activity is strictly sequence specific as mutation analysis showed the loss of ion channel function. Moreover, p7 ion channel activity can be specifically inhibited by different drugs suggesting the protein as a new target for future antiviral chemotherapy. In the present review, we focused to bring together the recent development to explore the potential role of p7 protein in HCV infection and its inhibition as a therapy.