tetano
Editor, Senior Moderator
Structure. 2016 Aug 9. pii: S0969-2126(16)30185-X. doi: 10.1016/j.str.2016.07.001. [Epub ahead of print]
[h=1]A Second RNA-Binding Site in the NS1 Protein of Influenza B Virus.[/h] Ma LC[SUP]1[/SUP], Guan R[SUP]1[/SUP], Hamilton K[SUP]1[/SUP], Aramini JM[SUP]1[/SUP], Mao L[SUP]1[/SUP], Wang S[SUP]2[/SUP], Krug RM[SUP]3[/SUP], Montelione GT[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza viruses cause a highly contagious respiratory disease in humans. The NS1 proteins of influenza A and B viruses (NS1A and NS1B proteins, respectively) are composed of two domains, a dimeric N-terminal domain and a C-terminal domain, connected by a flexible polypeptide linker. Here we report the 2.0-? X-ray crystal structure and nuclear magnetic resonance studies of the NS1B C-terminal domain, which reveal a novel and unexpected basic RNA-binding site that is not present in the NS1A protein. We demonstrate that single-site alanine replacements of basic residues in this site lead to reduced RNA-binding activity, and that recombinant influenza B viruses expressing these mutant NS1B proteins are severely attenuated in replication. This novel RNA-binding site of NS1B is required for optimal influenza B virus replication. Most importantly, this study reveals an unexpected RNA-binding function in the C-terminal domain of NS1B, a novel function that distinguishes influenza B viruses from influenza A viruses.
Copyright ? 2016 Elsevier Ltd. All rights reserved.
PMID: 27545620 DOI: 10.1016/j.str.2016.07.001
[PubMed - as supplied by publisher]
[h=1]A Second RNA-Binding Site in the NS1 Protein of Influenza B Virus.[/h] Ma LC[SUP]1[/SUP], Guan R[SUP]1[/SUP], Hamilton K[SUP]1[/SUP], Aramini JM[SUP]1[/SUP], Mao L[SUP]1[/SUP], Wang S[SUP]2[/SUP], Krug RM[SUP]3[/SUP], Montelione GT[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza viruses cause a highly contagious respiratory disease in humans. The NS1 proteins of influenza A and B viruses (NS1A and NS1B proteins, respectively) are composed of two domains, a dimeric N-terminal domain and a C-terminal domain, connected by a flexible polypeptide linker. Here we report the 2.0-? X-ray crystal structure and nuclear magnetic resonance studies of the NS1B C-terminal domain, which reveal a novel and unexpected basic RNA-binding site that is not present in the NS1A protein. We demonstrate that single-site alanine replacements of basic residues in this site lead to reduced RNA-binding activity, and that recombinant influenza B viruses expressing these mutant NS1B proteins are severely attenuated in replication. This novel RNA-binding site of NS1B is required for optimal influenza B virus replication. Most importantly, this study reveals an unexpected RNA-binding function in the C-terminal domain of NS1B, a novel function that distinguishes influenza B viruses from influenza A viruses.
Copyright ? 2016 Elsevier Ltd. All rights reserved.
PMID: 27545620 DOI: 10.1016/j.str.2016.07.001
[PubMed - as supplied by publisher]