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首页> 外文期刊>Fish & Shellfish Immunology >Sequence analysis and subcellular localization of crucian carp Carassius auratus viperin
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Sequence analysis and subcellular localization of crucian carp Carassius auratus viperin

机译：of鱼vi蛇毒蛇毒蛋白的序列分析和亚细胞定位

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摘要

Human viperin is known as an interferon (IFN)-inducible antiviral protein and localizes to endoplasmic reticulum (ER) via its N-terminal amphipathic alpha-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 alpha-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 alpha-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
机译：人毒蛇毒蛋白被称为干扰素（IFN）诱导型抗病毒蛋白，并通过其N末端两亲性α-螺旋定位于内质网（ER）。关于鱼毒蛋白的亚细胞定位知之甚少。在这里，我们表征了cru鱼Car鱼鱼毒蛋白的亚细胞定位。 sequence鱼viperin序列上与其他viperin蛋白几乎相同，但前N个末端的70个氨基酸被定义为包括两亲性α-螺旋的N末端可变域。除N端可变域外，cru鱼viperin蛋白还具有保守的中部自由基SAM域和保守的C端域。亚细胞定位分析表明cru鱼viperin是与ER相关的细胞质蛋白。序列分析显示氨基酸1-74形成两亲性α-螺旋结构域，该结构域驱动cru鱼viperin的ER定位。另外，共免疫沉淀试验表明cru鱼viperin蛋白能够自我结合。这些结果共同表明，与哺乳动物同源物相似，鱼类viperins可能在IFN反应中起重要作用

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