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

页码：30 / 38

页数：9