Identification of novel mutations in the methyltransferase complex (Nsp10-Nsp16) of SARS-CoV-2.
Identification of novel mutations in the methyltransferase complex (Nsp10-Nsp16) of SARS-CoV-2.
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DOI：
10.1016/j.bbrep.2020.100833
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发表时间：
2020-12
影响因子：
2.7
通讯作者：
Azad GK
中科院分区：
文献类型：
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作者：
Azad GK
最近爆发的大流行是由冠状病毒科的一个成员引起的，被确定为SARS-CoV-2。该病毒的高度传染性使其能够在全球范围内迅速传播，并造成严重的医疗保健和经济困境。到目前为止，还没有针对SARS-CoV-2的适当治疗方法或疫苗。自那以后，感染者迅速增加，导致冠状病毒病（COVID-19）患者的医疗系统饱和。随着病毒传播到新的地方，它也获得了各种突变。在这项研究中，我们重点鉴定了SARS-CoV-2的关键复合物之一Nsp 10-Nsp 16 2′-O-甲基转移酶复合物的突变。该复合物通过加帽在病毒RNA的转录后修饰中起着不可或缺的作用。我们分析了印度报道的208个Nsp 10-Nsp 16序列，并与中国武汉首次报道的序列进行了比较。我们的分析揭示了Nsp 10中的一个突变和Nsp 16蛋白中的五个突变。我们还表明，这些突变导致Nsp 10-Nsp 16二级结构的改变。此外，蛋白质建模研究表明，Nsp 10-Nsp 16的突变影响蛋白质的动态性和稳定性。总而言之，这项研究提供了新的见解，观察到的变化，在蛋白质的SARS-CoV-2，可能有功能的后果。SARS-CoV-2、Nsp 10和Nsp 16的非结构蛋白在传播到新的位置时发生突变。SARS-CoV-2在印度分离株中的Nsp 10-Nsp 16复合物中含有6个突变。这些突变改变了Nsp 10和Nsp 16的二级结构，也影响了蛋白质的动力学。
A recent outburst of the pandemic caused by a member of the coronaviridae family identified as SARS-CoV-2. The highly contagious nature of the virus allows it to spread rapidly worldwide and caused severe healthcare and economic distress. So far, no proper line of treatment or vaccines has been available against SARS-CoV-2. Since, the infected people rapidly increased, causing the saturation of healthcare systems with coronavirus disease (COVID-19) patients. As the virus spread to new locations it also acquired various mutations. Here, in this study, we focused on identifying mutations in one of the crucial complex of SARS-CoV-2, the Nsp10-Nsp16 2′-O-methyltransferase complex. This complex plays indispensable role in the post-transcriptional modifications of viral RNA by its capping. We analysed 208 sequences of Nsp10-Nsp16 reported from India and compared with first reported sequence from Wuhan, China. Our analysis revealed a single mutation in Nsp10 and five mutations in Nsp16 protein. We also show that these mutations are leading to alteration in the secondary structure of Nsp10-Nsp16. Further, the protein modelling studies revealed that the mutation of both Nsp10-Nsp16 impacts the protein dynamicity and stability. Altogether, this study provides novel insights into the variations observed in the proteins of SARS-CoV-2 that might have functional consequences. The non-structural protein of SARS-CoV-2, Nsp 10 and Nsp16 is mutated as it spreads to new locations. SARS-CoV-2 harbours six mutations in Nsp 10-Nsp16 complex among Indian Isolates. These mutation alters secondary structure of both Nsp 10 and Nsp16 and also affects protein dynamicity.
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影响因子：
6.7
作者：
Decroly E;Debarnot C;Ferron F;Bouvet M;Coutard B;Imbert I;Gluais L;Papageorgiou N;Sharff A;Bricogne G;Ortiz-Lombardia M;Lescar J;Canard B
通讯作者：
Canard B
影响因子：
11.3
作者：
Sola I;Almazán F;Zúñiga S;Enjuanes L
通讯作者：
Enjuanes L
影响因子：
7.6
作者：
Subissi L;Imbert I;Ferron F;Collet A;Coutard B;Decroly E;Canard B
通讯作者：
Canard B
影响因子：
14.9
作者：
Madeira, Fabio;Park, Young Mi;Lopez, Rodrigo
通讯作者：
Lopez, Rodrigo
DOI：
10.1074/jbc.m110.120014
发表时间：
2010-10-22
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Lugari A;Betzi S;Decroly E;Bonnaud E;Hermant A;Guillemot JC;Debarnot C;Borg JP;Bouvet M;Canard B;Morelli X;Lécine P
通讯作者：
Lécine P