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
中科院分区:
文献类型:
--
作者:
Zhang K;Wang Z;Liu X;Yin C;Basit Z;Xia B;Liu W
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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影响因子:
11.4
作者:
FUJIYOSHI, Y;KUME, NP;SATO, SB
通讯作者:
SATO, SB
影响因子:
5.4
作者:
Bui, M;Wills, EG;Whittaker, GR
通讯作者:
Whittaker, GR
影响因子:
5.4
作者:
Enami, M;Enami, K
通讯作者:
Enami, K
影响因子:
3.7
作者:
ENAMI, M;FUKUDA, R;ISHIHAMA, A
通讯作者:
ISHIHAMA, A
影响因子:
1.2
作者:
Ksenofontov, A. L.;Dobrov, E. N.;Baratova, L. A.
通讯作者:
Baratova, L. A.