tetano
Editor, Senior Moderator
PLoS One. 2017 Nov 16;12(11):e0188214. doi: 10.1371/journal.pone.0188214. eCollection 2017.
[h=1]Cellular hnRNP A2/B1 interacts with the NP of influenza A virus and impacts viral replication.[/h] Chang CK[SUP]1[/SUP], Chen CJ[SUP]2,[/SUP][SUP]3[/SUP], Wu CC[SUP]1,[/SUP][SUP]4,[/SUP][SUP]5[/SUP], Chen SW[SUP]2[/SUP], Shih SR[SUP]1,[/SUP][SUP]4,[/SUP][SUP]6,[/SUP][SUP]7[/SUP], Kuo RL[SUP]1,[/SUP][SUP]4,[/SUP][SUP]6,[/SUP][SUP]8[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The viral ribonucleoprotein (vRNP) of influenza A virus is formed by virion RNA (vRNA), viral polymerase complex, and nucleoprotein (NP). The NP plays an important role in facilitating the replication and stabilization of viral RNA. To explore host factors that may be involved in the regulation of viral replication through interactions with NP, we conducted an immunoprecipitation experiment followed by mass spectrometry to identify NP-associated cellular proteins. Here, we demonstrate that NP can interact and colocalize with heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1 in mammalian cells and that the interaction may occur via direct binding to the glycine-rich domain (GRD) of hnRNP A2/B1. In addition, two residues in the tail loop of NP, F412 and R422, are required for the interaction of hnRNP A2/B1. Because the knockdown of hnRNP A2/B1 expression reduces viral RNP activity, hnRNP A2/B1 may act as a positive regulator in viral RNA synthesis of influenza A virus. More importantly, the findings in this research demonstrate that host proteins can regulate the replication of influenza A virus by interacting with NP.
PMID: 29145464 DOI: 10.1371/journal.pone.0188214
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[h=1]Cellular hnRNP A2/B1 interacts with the NP of influenza A virus and impacts viral replication.[/h] Chang CK[SUP]1[/SUP], Chen CJ[SUP]2,[/SUP][SUP]3[/SUP], Wu CC[SUP]1,[/SUP][SUP]4,[/SUP][SUP]5[/SUP], Chen SW[SUP]2[/SUP], Shih SR[SUP]1,[/SUP][SUP]4,[/SUP][SUP]6,[/SUP][SUP]7[/SUP], Kuo RL[SUP]1,[/SUP][SUP]4,[/SUP][SUP]6,[/SUP][SUP]8[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The viral ribonucleoprotein (vRNP) of influenza A virus is formed by virion RNA (vRNA), viral polymerase complex, and nucleoprotein (NP). The NP plays an important role in facilitating the replication and stabilization of viral RNA. To explore host factors that may be involved in the regulation of viral replication through interactions with NP, we conducted an immunoprecipitation experiment followed by mass spectrometry to identify NP-associated cellular proteins. Here, we demonstrate that NP can interact and colocalize with heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1 in mammalian cells and that the interaction may occur via direct binding to the glycine-rich domain (GRD) of hnRNP A2/B1. In addition, two residues in the tail loop of NP, F412 and R422, are required for the interaction of hnRNP A2/B1. Because the knockdown of hnRNP A2/B1 expression reduces viral RNP activity, hnRNP A2/B1 may act as a positive regulator in viral RNA synthesis of influenza A virus. More importantly, the findings in this research demonstrate that host proteins can regulate the replication of influenza A virus by interacting with NP.
PMID: 29145464 DOI: 10.1371/journal.pone.0188214
Free full text