tetano
Editor, Senior Moderator
J Gen Virol. 2015 Feb 20. pii: vir.0.000095. doi: 10.1099/vir.0.000095. [Epub ahead of print]
[h=1]Mutation analysis of the RNA silencing suppressor NS1 encoded by avian influenza virus H9N2.[/h] Jing X[SUP]1[/SUP], Xu J[SUP]1[/SUP], Fan M[SUP]1[/SUP], Ma L[SUP]1[/SUP], Huang X[SUP]1[/SUP], Wang X[SUP]1[/SUP], Sun S[SUP]2[/SUP], Zhu C[SUP]1[/SUP], Liu H[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Non-structural protein 1 (NS1) binds siRNAs and suppresses RNA silencing in plants, but the underlying mechanism of this suppression is not well understood. Therefore, here we characterized NS1 encoded by the avian influenza virus H9N2. The NS1 protein was able to suppress RNA silencing induced by either sense RNA or double-stranded RNA (dsRNA). Using deletion and point mutants, we discovered that the first 70 residues of NS1 can suppress RNA silencing triggered by sense transgene, but this sequence is not sufficient to block dsRNA-induced silencing. Any mutations of two arginine residues (35R and 46R) of NS1, which contribute to its homodimeric structure, cause the loss of its silencing suppression activity. These results indicate that the region after residue 70 of NS1 is essential for the repression activity on dsRNA-induced RNA silencing, and that the dimeric structure of NS1 plays a critical role in its RNA silencing suppression function.
PMID: 25701825 [PubMed - as supplied by publisher]
[h=1]Mutation analysis of the RNA silencing suppressor NS1 encoded by avian influenza virus H9N2.[/h] Jing X[SUP]1[/SUP], Xu J[SUP]1[/SUP], Fan M[SUP]1[/SUP], Ma L[SUP]1[/SUP], Huang X[SUP]1[/SUP], Wang X[SUP]1[/SUP], Sun S[SUP]2[/SUP], Zhu C[SUP]1[/SUP], Liu H[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Non-structural protein 1 (NS1) binds siRNAs and suppresses RNA silencing in plants, but the underlying mechanism of this suppression is not well understood. Therefore, here we characterized NS1 encoded by the avian influenza virus H9N2. The NS1 protein was able to suppress RNA silencing induced by either sense RNA or double-stranded RNA (dsRNA). Using deletion and point mutants, we discovered that the first 70 residues of NS1 can suppress RNA silencing triggered by sense transgene, but this sequence is not sufficient to block dsRNA-induced silencing. Any mutations of two arginine residues (35R and 46R) of NS1, which contribute to its homodimeric structure, cause the loss of its silencing suppression activity. These results indicate that the region after residue 70 of NS1 is essential for the repression activity on dsRNA-induced RNA silencing, and that the dimeric structure of NS1 plays a critical role in its RNA silencing suppression function.
PMID: 25701825 [PubMed - as supplied by publisher]