title: PEDV ORF3 encodes an ion channel protein and regulates virus production.
abstract: Several studies suggest that the open reading frame 3 (ORF3) gene of porcine epidemic diarrhea virus (PEDV) is related to viral infectivity and pathogenicity, but its function remains unknown. Here, we propose a structure model of the ORF3 protein consisting of four TM domains and forming a tetrameric assembly. ORF3 protein can be detected in PEDV-infected cells and it functions as an ion channel in both Xenopus laevis oocytes and yeast. Mutation analysis showed that Tyr170 in TM4 is important for potassium channel activity. Furthermore, viral production is reduced in infected Vero cells when ORF3 gene is silenced by siRNA. Interestingly, the ORF3 gene from an attenuated PEDV encodes a truncated protein with 49 nucleotide deletions, which lacks the ion channel activity.
authors.affiliation: Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.
authors.forename: Kai
authors.initials: K
authors.lastname: Wang
authors.forename: Wei
authors.initials: W
authors.lastname: Lu
authors.forename: Jianfei
authors.initials: J
authors.lastname: Chen
authors.forename: Shiqi
authors.initials: S
authors.lastname: Xie
authors.forename: Hongyan
authors.initials: H
authors.lastname: Shi
authors.forename: Haojen
authors.initials: H
authors.lastname: Hsu
authors.forename: Wenjing
authors.initials: W
authors.lastname: Yu
authors.forename: Ke
authors.initials: K
authors.lastname: Xu
authors.forename: Chao
authors.initials: C
authors.lastname: Bian
authors.forename: Wolfgang B
authors.initials: WB
authors.lastname: Fischer
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Schwarz
authors.forename: Li
authors.initials: L
authors.lastname: Feng
authors.forename: Bing
authors.initials: B
authors.lastname: Sun
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D001483:Base Sequence; D002522:Chlorocebus aethiops; D004279:DNA, Viral / Q000235:genetics; D005260:Female; D005816:Genetic Complementation Test; D007473:Ion Channels / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009865:Oocytes / Q000378:metabolism; D016366:Open Reading Frames; D053485:Porcine epidemic diarrhea virus / Q000235:genetics* / Q000472:pathogenicity / Q000502:physiology*; D011487:Protein Conformation; D034741:RNA, Small Interfering / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D014709:Vero Cells; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D014774:Virulence / Q000235:genetics / Q000502:physiology; D014779:Virus Replication / Q000235:genetics / Q000502:physiology; D014982:Xenopus laevis
chemical_list: D004279:DNA, Viral; D007473:Ion Channels; D034741:RNA, Small Interfering; D011994:Recombinant Proteins; D014764:Viral Proteins