tetano
Editor, Senior Moderator
Biochem Biophys Res Commun. 2013 Dec 19. pii: S0006-291X(13)02140-2. doi: 10.1016/j.bbrc.2013.12.071. [Epub ahead of print]
Involvement of the N-terminal portion of influenza virus RNA polymerase subunit PB1 in nucleotide recognition.
Binh NT1, Wakai C2, Kawaguchi A3, Nagata K4.
Author information
Abstract
The influenza virus PB1 protein functions as a catalytic subunit of the viral RNA-dependent RNA polymerase and contains the highly conserved motifs of RNA-dependent RNA polymerases together with putative nucleotide-binding sites. PB1 also binds to viral genomic RNAs and its replicative intermediates through the promoter regions. The detail function and interplay between functional domains are not clarified although a part of structures and functions of PB1 have been clarified. In this study, we analyzed the function of PB1 subunit in the sense of nucleotide recognition using ribavirin, which is a nucleoside analog and inhibits viral RNA synthesis of many RNA viruses including influenza virus. We screened ribavirin-resistant PB1 mutants from randomly mutated PB1 cDNA library using a mini-replicon assay, and we identified a single mutation at the amino acid position 27 of PB1 as an important residue for the nucleotide recognition.
Copyright ? 2013. Published by Elsevier Inc.
KEYWORDS:
influenza, nucleotide recognition, resistant mutant, ribavirin
PMID:
24361882
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24361882
Involvement of the N-terminal portion of influenza virus RNA polymerase subunit PB1 in nucleotide recognition.
Binh NT1, Wakai C2, Kawaguchi A3, Nagata K4.
Author information
Abstract
The influenza virus PB1 protein functions as a catalytic subunit of the viral RNA-dependent RNA polymerase and contains the highly conserved motifs of RNA-dependent RNA polymerases together with putative nucleotide-binding sites. PB1 also binds to viral genomic RNAs and its replicative intermediates through the promoter regions. The detail function and interplay between functional domains are not clarified although a part of structures and functions of PB1 have been clarified. In this study, we analyzed the function of PB1 subunit in the sense of nucleotide recognition using ribavirin, which is a nucleoside analog and inhibits viral RNA synthesis of many RNA viruses including influenza virus. We screened ribavirin-resistant PB1 mutants from randomly mutated PB1 cDNA library using a mini-replicon assay, and we identified a single mutation at the amino acid position 27 of PB1 as an important residue for the nucleotide recognition.
Copyright ? 2013. Published by Elsevier Inc.
KEYWORDS:
influenza, nucleotide recognition, resistant mutant, ribavirin
PMID:
24361882
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24361882