title: Identification of peptides that bind hepatitis C virus envelope protein E2 and inhibit viral cellular entry from a phage-display peptide library.
abstract: Hepatitis C virus (HCV) envelope protein E2 is required for the entry of HCV into cells. Viral envelope proteins interact with cell receptors in a multistep process, which may be a promising target for the development of novel antiviral agents. In this study, a heptapeptide M13 phage-display library was screened for peptides that bind specifically to prokaryotically expressed, purified truncated HCV envelope protein E2. ELISA assay was used to quantify the binding of the peptides to HCV E2 protein. Flow cytometry, quantitative reverse-transcription PCR and western blotting were used to investigate the inhibition effect of one peptide on HCV infection in hepatoma cells (Huh7.5) in vitro. Four peptides capable of binding specifically to HCV E2 protein were obtained after three rounds of biopanning. Peptide C18 (WPWHNHR), with the highest affinity for binding HCV E2 protein, was synthesized. The results showed that peptide C18 inhibited the viral infectivity of both HCV pseudotype particles (HCVpp) harboring HCV envelope glycoproteins and cell-culture produced HCV (HCVcc). Thus, this study demonstrated that peptide C18 is a potential candidate for anti-HCV therapy as a novel viral entry inhibitor.
authors.affiliation: Department of Microbiology, the Fourth Military Medical University, Xi'an, Shaanxi 710032, P.R. China.
authors.forename: Xin
authors.initials: X
authors.lastname: Lü
authors.affiliation: Department of Microbiology, the Fourth Military Medical University, Xi'an, Shaanxi 710032, P.R. China.
authors.forename: Min
authors.initials: M
authors.lastname: Yao
authors.affiliation: Department of Microbiology, the Fourth Military Medical University, Xi'an, Shaanxi 710032, P.R. China.
authors.forename: Jian-Min
authors.initials: JM
authors.lastname: Zhang
authors.affiliation: Department of Microbiology, the Fourth Military Medical University, Xi'an, Shaanxi 710032, P.R. China.
authors.forename: Jing
authors.initials: J
authors.lastname: Yang
authors.affiliation: Department of Microbiology, the Fourth Military Medical University, Xi'an, Shaanxi 710032, P.R. China.
authors.forename: Ying-Feng
authors.initials: YF
authors.lastname: Lei
authors.affiliation: Department of Microbiology, the Fourth Military Medical University, Xi'an, Shaanxi 710032, P.R. China.
authors.forename: Xiao-Jun
authors.initials: XJ
authors.lastname: Huang
authors.affiliation: Center of Diagnosis and Treatment for Infectious Disease of Chinese PLA, Tangdu Hospital, the Fourth Military Medical University, Xi'an, Shaanxi 710038, P.R. China.
authors.forename: Zhan-Sheng
authors.initials: ZS
authors.lastname: Jia
authors.affiliation: Center of Diagnosis and Treatment for Infectious Disease of Chinese PLA, Tangdu Hospital, the Fourth Military Medical University, Xi'an, Shaanxi 710038, P.R. China.
authors.forename: Li
authors.initials: L
authors.lastname: Ma
authors.affiliation: Department of Microbiology, the Fourth Military Medical University, Xi'an, Shaanxi 710032, P.R. China.
authors.forename: Hai-Yun
authors.initials: HY
authors.lastname: Lan
authors.affiliation: Department of Microbiology, the Fourth Military Medical University, Xi'an, Shaanxi 710032, P.R. China.
authors.forename: Zhi-Kai
authors.initials: ZK
authors.lastname: Xu
authors.affiliation: Department of Microbiology, the Fourth Military Medical University, Xi'an, Shaanxi 710032, P.R. China.
authors.forename: Wen
authors.initials: W
authors.lastname: Yin
mesh_terms: D000998:Antiviral Agents / Q000494:pharmacology*; D002460:Cell Line; D016174:Hepacivirus / Q000187:drug effects* / Q000378:metabolism*; D006801:Humans; D019151:Peptide Library; D010455:Peptides / Q000494:pharmacology*; D014759:Viral Envelope Proteins / Q000378:metabolism*; D053586:Virus Internalization / Q000187:drug effects
chemical_list: D000998:Antiviral Agents; D019151:Peptide Library; D010455:Peptides; D014759:Viral Envelope Proteins