Open AccessTranslational Inhibition and Increased Interferon Induction in Cells Infected with C Protein-Deficient Measles Virus
Author(s) -
Yuichiro Nakatsu,
Makoto Takeda,
Shinji Ohno,
Ritsuko Koga,
Yusuke Yanagi
Publication year - 2006
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00751-06
Subject(s) - biology , measles virus , protein kinase r , interferon , virology , protein biosynthesis , microbiology and biotechnology , internal ribosome entry site , viral replication , initiation factor , virus , phosphoprotein , rna , paramyxoviridae , antiviral protein , translation (biology) , eukaryotic translation , protein kinase a , phosphorylation , messenger rna , gene , cyclin dependent kinase 2 , biochemistry , measles , vaccination , viral disease
In addition to the phosphoprotein, the P gene of measles virus (MV) also encodes the V and C proteins by an RNA editing process and by alternative initiation of translation in a different reading frame, respectively. Although the MV C protein is required for efficient MV replication in vivo and in some cultured cells, its exact functions in virus infection are currently unclear. Here, we report that a recombinant MV lacking the C protein (MVΔC) grew poorly in a human cell line possessing the intact interferon (IFN) pathway and that this growth defect was associated with reduced viral translation and genome replication. The translational inhibition was correlated with phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. Moreover, increased IFN induction was observed in MVΔC-infected cells. The NS1 protein of influenza virus, which binds to double-stranded RNA (dsRNA) and consequently inhibits IFN induction and dsRNA-dependent protein kinase activation, complemented the growth defect of MVΔC. These results indicate that the MV C protein inhibits IFN induction and modulates host antiviral responses, thereby ensuring MV growth in host cells.