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Virology. 2018 May 15;520:30-38. doi: 10.1016/j.virol.2018.05.002. [Epub ahead of print]
Phosphorylation and dephosphorylation of threonine 188 in nucleoprotein is crucial for the replication of influenza A virus.
Li Y1, Sun L2, Zheng W3, Madina Mahesutihan4, Li J4, Bi Y3, Wang H5, Liu W6, Luo TR7.
Author information
Abstract
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.
KEYWORDS:
Influenza A virus; Nucleoprotein; Phosphorylation; Viral replication
PMID: 29775781 DOI: 10.1016/j.virol.2018.05.002
Phosphorylation and dephosphorylation of threonine 188 in nucleoprotein is crucial for the replication of influenza A virus.
Li Y1, Sun L2, Zheng W3, Madina Mahesutihan4, Li J4, Bi Y3, Wang H5, Liu W6, Luo TR7.
Author information
Abstract
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.
KEYWORDS:
Influenza A virus; Nucleoprotein; Phosphorylation; Viral replication
PMID: 29775781 DOI: 10.1016/j.virol.2018.05.002