The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein.

The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein.
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SARS冠状病毒的“ SARS唯一结构域”(SUD)是寡核(G)结合蛋白。

DOI:
10.1016/j.bbrc.2007.10.081
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发表时间:
2007-12-28
影响因子:
3.1
通讯作者:
Schmidt CL
Schmidt CL
中科院分区:
生物学4区
文献类型:
--
作者:
Tan J;Kusov Y;Mutschall D;Tech S;Nagarajan K;Hilgenfeld R;Schmidt CL

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严重急性呼吸道综合征(SARS)是一种由新型冠状病毒引起的高度传染性疾病,于2003年出现,死亡人数众多。SARS冠状病毒(SARS-CoV)对人类异常高的致病性的分子原因仍然是未知的。为了表征其他冠状病毒中不存在的病毒分子组分,所有这些冠状病毒对人类的致病性都要低得多,我们在SARS-CoV的非结构蛋白3(Nsp 3)内重组产生了SARS独特结构域(SUD),并表征了其核酸结合特性。区带干扰凝胶电泳和电泳迁移率变动分析表明,SUD的寡(G)-字符串的特异性亲和力。一些这样的片段存在于SARS-CoV基因组中,但也存在于参与信号传导途径调节的宿主蛋白质的mRNA中。SUD在病毒诱导的宿主细胞凋亡或存活中的假定作用进行了讨论。
Caused by a new coronavirus, severe acute respiratory syndrome (SARS) is a highly contagious disease associated with significant fatality that emerged in 2003. The molecular cause of the unusually high human pathogenicity of the SARS coronavirus (SARS-CoV) is still unknown. In an effort to characterize molecular components of the virus that are absent in other coronaviruses, all of which are considerably less pathogenic for humans, we recombinantly produced the SARS-unique domain (SUD) within non-structural protein 3 (Nsp3) of SARS-CoV and characterized its nucleic-acid binding properties. Zone-interference gel electrophoresis and electrophoretic mobility shift assays revealed a specific affinity of SUD for oligo(G)-strings. A few such segments are present in the SARS-CoV genome, but also in mRNAs of host proteins involved in the regulation of signaling pathways. A putative role of SUD in virus-induced apoptosis or survival of host cells is discussed.
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