Phosphorylation and dephosphorylation of threonine 188 in nucleoprotein is crucial for the replication of influenza A virus

被引：17
|
作者：
Li, Yun [1 ,2 ,3 ]
Sun, Lei [3 ,4 ]
Zheng, Weinan [3 ]
Mahesutihan, Madina [3 ,4 ]
Li, Jing [3 ,4 ]
Bi, Yuhai [3 ]
Wang, Heran [5 ]
Liu, Wenjun [1 ,2 ,3 ,4 ]
Luo, Ting Rong [1 ,2 ]
机构：
[1] Guangxi Univ, Coll Anim Sci & Vet Med, State Key Lab Conservat & Utilizat Subtrop AgroBi, Nanning 530004, Guangxi, Peoples R China
[2] Guangxi Univ, Coll Anim Sci & Vet Med, Lab Anim Infect Dis, Nanning 530004, Guangxi, Peoples R China
[3] Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China
[4] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[5] Beijing Natl Day Sch, Int Dept, Beijing 100039, Peoples R China
来源：
VIROLOGY | 2018年 / 520卷
基金：
中国国家自然科学基金;
关键词：
Nucleoprotein; Influenza A virus; Phosphorylation; Viral replication; NUCLEAR IMPORT; VIRAL REPLICATION; MESSENGER-RNA; AMINO-ACIDS; PROTEIN; IDENTIFICATION; OLIGOMERIZATION; BINDING; RIBONUCLEOPROTEIN; POLYMERASE;
D O I：
10.1016/j.virol.2018.05.002
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
Nucleoprotein (NP) is a major component of the viral ribonucleoprotein (vRNP) complex that is responsible for viral replication, transcription and packaging of influenza A virus. Phosphorylation of NP plays an important role during viral infection. In the present study, we identified threonine 188 (T188) as a novel phosphorylated residue in the NP of influenza A virus by using mass spectrometry. T188 is located within nuclear export signal 2 (NES2) which is chromosome region maintenance 1 (CRM1)-independent. We observed that the phosphorylation and dephosphorylation of residue T188 regulated viral replication by controlling NES2-dependent NP nuclear export and the polymerase activity of the vRNP complex. Our findings provide further insights for understanding the replication of influenza A virus.
引用
收藏
页码：30 / 38
页数：9
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