Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domain.

Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domain.
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甲型流感病毒 M1 蛋白的剖析:N 端结构域的 pH 依赖性寡聚化和 C 端结构域的二聚化

DOI:
10.1371/journal.pone.0037786
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Liu W
Liu W
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Zhang K;Wang Z;Liu X;Yin C;Basit Z;Xia B;Liu W

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背景甲型流感病毒基质1(M1)蛋白在整个病毒生命周期中起着重要作用。M1的寡聚化对于组装和出芽过程中病毒基质层的形成至关重要。方法/主要发现在本研究中,我们报告说,M1可以在体外寡聚化,寡聚化是pH值依赖性的。在pH 7.4时,M1的N-末端结构域单独作为多级低聚物存在,C-末端结构域单独形成唯一稳定的二聚体。因此,完整的M1可以显示不同形式的寡聚体和二聚体是最小的寡聚化状态,在中性pH值。在pH值5.0时,N-末端结构域的寡聚体完全解离成单体,而C-末端结构域保持在二聚体形式。其结果是,完整的M1的低聚物解离成一个稳定的二聚体在酸性pH值。结论/意义寡聚化的M1涉及的N-和C-末端结构域。N端结构域决定了pH依赖性寡聚化特征,C端结构域形成稳定的二聚体,这有助于M1的二聚化。本研究将有助于揭示甲型流感病毒的组装和脱壳过程的机制。
Background The matrix 1 (M1) protein of Influenza A virus plays many critical roles throughout the virus life cycle. The oligomerization of M1 is essential for the formation of the viral matrix layer during the assembly and budding process. Methodology/Principal Findings In the present study, we report that M1 can oligomerize in vitro, and that the oligomerization is pH-dependent. The N-terminal domain of M1 alone exists as multiple-order oligomers at pH 7.4, and the C-terminal domain alone forms an exclusively stable dimer. As a result, intact M1 can display different forms of oligomers and dimer is the smallest oligomerization state, at neutral pH. At pH 5.0, oligomers of the N-terminal domain completely dissociate into monomers, while the C-terminal domain remains in dimeric form. As a result, oligomers of intact M1 dissociate into a stable dimer at acidic pH. Conclusions/Significance Oligomerization of M1 involves both the N- and C-terminal domains. The N-terminal domain determines the pH-dependent oligomerization characteristic, and C-terminal domain forms a stable dimer, which contributes to the dimerization of M1. The present study will help to unveil the mechanisms of influenza A virus assembly and uncoating process.
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