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火鸡鼻气管炎病毒:体内和体外多肽合成

Turkey rhinotracheitis virus: in vivo and in vitro polypeptide synthesis.

作者信息

Ling R, Pringle C R

机构信息

Department of Biological Sciences, University of Warwick, Coventry, U.K.

出版信息

J Gen Virol. 1988 Apr;69 ( Pt 4):917-23. doi: 10.1099/0022-1317-69-4-917.

DOI:10.1099/0022-1317-69-4-917
PMID:3356982
Abstract

Turkey rhinotracheitis (TRT) virus is a paramyxovirus associated with recent outbreaks of acute respiratory disease in turkeys. On morphological criteria it resembles the pneumoviruses more than the other members of the paramyxovirus family. In this communication we report the identification of five virus-induced polypeptides in TRT virus-infected BS-C-1 cells. The Mr of these polypeptides were estimated as 38K, 35K, 30K, 19K and 15K from their electrophoretic mobility in SDS-polyacrylamide 6 to 15% gradient gels. The virus specificity of four (the 38K, 35K, 30K and 19K Mr polypeptides) of these five was confirmed by their predominance as products of in vitro translation of mRNA from TRT virus-infected BS-C-1 cells. An additional virus-specific polypeptide with an estimated Mr of 22K was revealed by in vitro translation and may be either a non-structural polypeptide or a minor structural protein. All six polypeptides were immunoprecipitated by a murine antiserum. Three other polypeptides (129K, 57K and 45K) were also immunoprecipitated. The 57K, 45K and 15K Mr polypeptides were glycosylated, and the 57K glycopolypeptide may be a disulphide-bonded dimer of the 45K and 15K glycopolypeptides. Another major glycopolypeptide of 83K Mr was observed but its virus-specificity could not be confirmed. Taken together our results tentatively identify eight or nine TRT virus-specified polypeptides and are consistent with the classification of TRT virus as a new member of the genus Pneumovirus.

摘要

火鸡鼻气管炎(TRT)病毒是一种副粘病毒,与近期火鸡急性呼吸道疾病的爆发有关。根据形态学标准,它比副粘病毒科的其他成员更类似于肺病毒。在本通讯中,我们报告了在TRT病毒感染的BS-C-1细胞中鉴定出五种病毒诱导的多肽。根据它们在SDS-聚丙烯酰胺6%至15%梯度凝胶中的电泳迁移率,这些多肽的相对分子质量估计为38K、35K、30K、19K和15K。这五种多肽中的四种(相对分子质量为38K、35K、30K和19K的多肽)的病毒特异性通过它们作为TRT病毒感染的BS-C-1细胞mRNA体外翻译产物的优势得到证实。体外翻译揭示了一种估计相对分子质量为22K的额外病毒特异性多肽,它可能是一种非结构多肽或一种次要结构蛋白。所有六种多肽都被鼠抗血清免疫沉淀。另外三种多肽(129K、57K和45K)也被免疫沉淀。相对分子质量为57K、45K和15K的多肽被糖基化,并且57K糖多肽可能是45K和15K糖多肽的二硫键连接的二聚体。观察到另一种相对分子质量为83K的主要糖多肽,但其病毒特异性无法得到证实。综上所述,我们的结果初步鉴定出八或九种TRT病毒特异性多肽,并且与将TRT病毒分类为肺病毒属的新成员一致。

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