Conservation of hydrophobicity within viral envelope glycoproteins reveals a putative hepatitis C virus fusion peptide

Journal article

The mechanism(s) by which hepatitis C virus (HCV) enters and infects cells remains unknown. Identifying the HCV fusion peptide(s) and understanding the early stages of infection may provide new opportunities for improved antiviral therapy. The HCV envelope glycoprotein E2 is thought to be a class II fusion protein. Class II fusion proteins are exemplified by the E protein of the tick-borne encephalitis virus (TBEV) and the E1 protein of the Semliki Forest virus (SFV). Analysis of the hydropho...

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Authors: Taylor, A; O'Leary, J; Pollock, S; Zitzmann, N

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: Bentham Science Publishers Publisher's website
• Journal: Protein and Peptide Letters Journal website
• Volume: 16
• Issue: 7
• Pages: 815-822
• Publication date: 2009-07-01
• DOI: 10.2174/092986609788681779
• EISSN: 1875-5305
• ISSN: 0929-8665
• Language: English
• Keywords: hepacivirus; viral envelope proteins; virus internalization; viral fusion proteins; liposomes; togaviridae; amino acid sequence; protein conformation; conserved sequence; molecular sequence data; models, molecular; phylogeny; hydrophobic and hydrophilic interactions; peptides