Influenza A Virus NS1 Protein Binds as a Dimer to RNA-Free PABP1 but Not to the PABP1·Poly(A) RNA Complex,Biochemistry

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Influenza A Virus NS1 Protein Binds as a Dimer to RNA-Free PABP1 but Not to the PABP1·Poly(A) RNA Complex
Biochemistry ( IF 2.9 ) Pub Date : 2020-11-10 , DOI: 10.1021/acs.biochem.0c00666
Cyrus M de Rozières ₁ , Simpson Joseph ₁

Affiliation

Influenza A virus (IAV) is a highly contagious human pathogen that is responsible for tens of thousands of deaths each year. Non-structural protein 1 (NS1) is a crucial protein expressed by IAV to evade the host immune system. Additionally, NS1 has been proposed to stimulate translation because of its ability to bind poly(A) binding protein 1 (PABP1) and eukaryotic initiation factor 4G. We analyzed the interaction of NS1 with PABP1 using quantitative techniques. Our studies show that NS1 binds as a homodimer to PABP1, and this interaction is conserved across different IAV strains. Unexpectedly, NS1 does not bind to PABP1 that is bound to poly(A) RNA. Instead, NS1 binds only to PABP1 free of RNA, suggesting that stimulation of translation does not occur by NS1 interacting with the PABP1 molecule attached to the mRNA 3′-poly(A) tail. These results suggest that the function of the NS1·PABP1 complex appears to be distinct from the classical role of PABP1 in translation initiation, when it is bound to the 3′-poly(A) tail of mRNA.

中文翻译：

甲型流感病毒 NS1 蛋白以二聚体形式与无 RNA 的 PABP1 结合，但不与 PABP1·Poly(A) RNA 复合物结合

甲型流感病毒 (IAV) 是一种高度传染性的人类病原体，每年导致数万人死亡。非结构蛋白 1 (NS1) 是 IAV 表达以逃避宿主免疫系统的关键蛋白质。此外，由于 NS1 能够结合 poly(A) 结合蛋白 1 (PABP1) 和真核起始因子 4G，因此有人建议 NS1 刺激翻译。我们使用定量技术分析了 NS1 与 PABP1 的相互作用。我们的研究表明 NS1 作为同型二聚体与 PABP1 结合，并且这种相互作用在不同的 IAV 菌株中是保守的。出乎意料的是，NS1 不与 PABP1 结合，而 PABP1 与 poly(A) RNA 结合。相反，NS1 仅与不含 RNA 的 PABP1 结合，这表明 NS1 与连接到 mRNA 3'-poly(A) 尾部的 PABP1 分子相互作用不会刺激翻译。

更新日期：2020-11-25

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