tetano
Editor, Senior Moderator
Virology. 2018 May 15;520:30-38. doi: 10.1016/j.virol.2018.05.002. [Epub ahead of print]
[h=1]Phosphorylation and dephosphorylation of threonine 188 in nucleoprotein is crucial for the replication of influenza A virus.[/h] Li Y[SUP]1[/SUP], Sun L[SUP]2[/SUP], Zheng W[SUP]3[/SUP], Madina Mahesutihan[SUP]4[/SUP], Li J[SUP]4[/SUP], Bi Y[SUP]3[/SUP], Wang H[SUP]5[/SUP], Liu W[SUP]6[/SUP], Luo TR[SUP]7[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
[h=4]KEYWORDS:[/h] Influenza A virus; Nucleoprotein; Phosphorylation; Viral replication
PMID: 29775781 DOI: 10.1016/j.virol.2018.05.002
[h=1]Phosphorylation and dephosphorylation of threonine 188 in nucleoprotein is crucial for the replication of influenza A virus.[/h] Li Y[SUP]1[/SUP], Sun L[SUP]2[/SUP], Zheng W[SUP]3[/SUP], Madina Mahesutihan[SUP]4[/SUP], Li J[SUP]4[/SUP], Bi Y[SUP]3[/SUP], Wang H[SUP]5[/SUP], Liu W[SUP]6[/SUP], Luo TR[SUP]7[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
[h=4]KEYWORDS:[/h] Influenza A virus; Nucleoprotein; Phosphorylation; Viral replication
PMID: 29775781 DOI: 10.1016/j.virol.2018.05.002