Sequence analysis and subcellular localization of crucian carp Carassius auratus viperin.
Human viperin is known as an interferon (IFN)-inducible antiviral protein and localizes to endoplasmic reticulum (ER) via its N-terminal amphipathic α-helix. Little is known about subcellular localization of fish viperin. Herein, we characterized subcellular localization of a fish viperin from crucian carp Carassius auratus. Crucian carp viperin is nearly identical to the other viperin proteins in sequence, with the exception of the first N-terminal 70 amino acids that are defined as N-terminal variable domain including an amphipathic α-helix. In addition to N-terminal variable domain, crucian carp viperin protein harbors a conserved middle radical SAM domain and a conserved C-terminal domain. Subcellular localization analyses indicate that crucian carp viperin is a cytoplasmic protein associated with ER. Sequence analyses reveal that amino acids 1-74 forms an amphipathic α-helix domain that drives ER-localization of crucian carp viperin. In addition, Coimmunoprecipitation assays show that crucian carp viperin proteins are able to self-associate. These results together indicate that similar to mammalian homologs, fish viperins likely play important roles in IFN response.
State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Wuhan 430072, China.
Bing
B
Wang
State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Wuhan 430072, China. Electronic address: ybzhang@ihb.ac.cn.
Yi-Bing
YB
Zhang
State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Wuhan 430072, China.
Ting-Kai
TK
Liu
State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Wuhan 430072, China. Electronic address: jfgui@ihb.ac.cn.
Jian-Fang
JF
Gui
D000818:Animals; D001483:Base Sequence; D002347:Carps / Q000235:genetics*; D017124:Conserved Sequence / Q000235:genetics; D004721:Endoplasmic Reticulum / Q000378:metabolism; D029941:Fish Proteins / Q000235:genetics*; D047468:Immunoprecipitation; D008969:Molecular Sequence Data; D044925:Oxidoreductases Acting on CH-CH Group Donors; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000235:genetics; D017422:Sequence Analysis, DNA; D013045:Species Specificity; D000090123:Viperin Protein
D029941:Fish Proteins; D044925:Oxidoreductases Acting on CH-CH Group Donors; D011506:Proteins; C444427:RSAD2 protein, human; D000090123:Viperin Protein
Carassius auratus; Cytoplasmic localization; Endoplasmic reticulum localization; Self-association; Viperin