tetano
Editor, Senior Moderator
Biochem Biophys Res Commun. 2013 Dec 2. pii: S0006-291X(13)02002-0. doi: 10.1016/j.bbrc.2013.11.100. [Epub ahead of print]
Nucleoprotein of influenza B virus binds to its type A counterpart and disrupts influenza A viral polymerase complex formation.
Jaru-Ampornpan P, Narkpuk J, Wanitchang A, Jongkaewwattana A.
Source
Virology and Cell Technology Laboratory, National Center for Genetic Engineering and Biotechnology (BIOTEC), Pathumthani, Thailand. Electronic address: peera.jar@biotec.or.th.
Abstract
Upon co-infection with influenza B virus (FluB), influenza A virus (FluA) replication is substantially impaired. Previously, we have shown that the nucleoprotein of FluB (BNP) can inhibit FluA polymerase machinery, retarding the growth of FluA. However, the molecular mechanism underlying this inhibitory action awaited further investigation. Here, we provide evidence that BNP hinders the proper formation of FluA polymerase complex by competitively binding to the nucleoprotein of FluA. To exert this inhibitory effect, BNP must be localized in the nucleus. The interaction does not require the presence of the viral RNA but needs an intact BNP RNA-binding motif. The results highlight the novel role of BNP as an anti-influenza A viral agent and provide insights into the mechanism of intertypic interference.
Copyright ? 2013. Published by Elsevier Inc.
KEYWORDS:
gene reassortment, influenza virus, intertypic interference, nucleoprotein
PMID:
24309113
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24309113
Nucleoprotein of influenza B virus binds to its type A counterpart and disrupts influenza A viral polymerase complex formation.
Jaru-Ampornpan P, Narkpuk J, Wanitchang A, Jongkaewwattana A.
Source
Virology and Cell Technology Laboratory, National Center for Genetic Engineering and Biotechnology (BIOTEC), Pathumthani, Thailand. Electronic address: peera.jar@biotec.or.th.
Abstract
Upon co-infection with influenza B virus (FluB), influenza A virus (FluA) replication is substantially impaired. Previously, we have shown that the nucleoprotein of FluB (BNP) can inhibit FluA polymerase machinery, retarding the growth of FluA. However, the molecular mechanism underlying this inhibitory action awaited further investigation. Here, we provide evidence that BNP hinders the proper formation of FluA polymerase complex by competitively binding to the nucleoprotein of FluA. To exert this inhibitory effect, BNP must be localized in the nucleus. The interaction does not require the presence of the viral RNA but needs an intact BNP RNA-binding motif. The results highlight the novel role of BNP as an anti-influenza A viral agent and provide insights into the mechanism of intertypic interference.
Copyright ? 2013. Published by Elsevier Inc.
KEYWORDS:
gene reassortment, influenza virus, intertypic interference, nucleoprotein
PMID:
24309113
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24309113