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Nat Commun. 2014 Feb 10;5:3259. doi: 10.1038/ncomms4259.
Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus.
Zhou Z1, Cao M1, Guo Y1, Zhao L2, Wang J2, Jia X2, Li J2, Wang C2, Gabriel G3, Xue Q2, Yi Y4, Cui S2, Jin Q2, Wang J2, Deng T2.
Author information
Abstract
The ribonucleoprotein (RNP) of the influenza A virus is responsible for the transcription and replication of viral RNA in the nucleus. These processes require interplay between host factors and RNP components. Here, we report that the Fragile X mental retardation protein (FMRP) targets influenza virus RNA synthesis machinery and facilitates virus replication both in cell culture and in mice. We demonstrate that FMRP transiently associates with viral RNP and stimulates viral RNP assembly through RNA-mediated interaction with the nucleoprotein. Furthermore, the KH2 domain of FMRP mediates its association with the nucleoprotein. A point mutation (I304N) in the KH2 domain, identified from a Fragile X syndrome patient, disrupts the FMRP-nucleoprotein association and abolishes the ability of FMRP to participate in viral RNP assembly. We conclude that FMRP is a critical host factor used by influenza viruses to facilitate viral RNP assembly. Our observation reveals a mechanism of influenza virus RNA synthesis and provides insights into FMRP functions.
PMID:
24514761
[PubMed - in process]
Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus.
Zhou Z1, Cao M1, Guo Y1, Zhao L2, Wang J2, Jia X2, Li J2, Wang C2, Gabriel G3, Xue Q2, Yi Y4, Cui S2, Jin Q2, Wang J2, Deng T2.
Author information
Abstract
The ribonucleoprotein (RNP) of the influenza A virus is responsible for the transcription and replication of viral RNA in the nucleus. These processes require interplay between host factors and RNP components. Here, we report that the Fragile X mental retardation protein (FMRP) targets influenza virus RNA synthesis machinery and facilitates virus replication both in cell culture and in mice. We demonstrate that FMRP transiently associates with viral RNP and stimulates viral RNP assembly through RNA-mediated interaction with the nucleoprotein. Furthermore, the KH2 domain of FMRP mediates its association with the nucleoprotein. A point mutation (I304N) in the KH2 domain, identified from a Fragile X syndrome patient, disrupts the FMRP-nucleoprotein association and abolishes the ability of FMRP to participate in viral RNP assembly. We conclude that FMRP is a critical host factor used by influenza viruses to facilitate viral RNP assembly. Our observation reveals a mechanism of influenza virus RNA synthesis and provides insights into FMRP functions.
PMID:
24514761
[PubMed - in process]
