期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 8, 页码 4748-4758出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M114.602649
关键词
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资金
- Biotechnology and Biological Sciences Research Council [BB/I01232X/1, BB/I012303/1, BB/H009728/1]
- Wellcome Trust [WT097997MA]
- Majlis Amanah Rakyat (MARA), Government of Malaysia
- University of Kuala Lumpur
- BBSRC [BB/I012303/1, BB/H009728/1, BB/I01232X/1, BB/L018209/1, BB/H018956/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H018956/1, BB/L018209/1, BB/I012303/1, BB/I01232X/1, BB/H009728/1] Funding Source: researchfish
Protein synthesis is a tightly controlled process responding to several stimuli, including viral infection. As obligate intracellular parasites, viruses depend on the translation machinery of the host and can manipulate it by affecting the availability and function of specific eukaryotic initiation factors (eIFs). Human norovirus is a member of the Caliciviridae family and is responsible for gastroenteritis outbreaks. Previous studies on feline calicivirus and murine norovirus 1 (MNV1) demonstrated that the viral protein, genome-linked (VPg), acts to direct translation by hijacking the host protein synthesis machinery. Here we report that MNV1 infection modulates the MAPK pathway to activate eIF4E phosphorylation. Our results show that the activation of p38 and Mnk during MNV1 infection is important for MNV1 replication. Furthermore, phosphorylated eIF4E relocates to the polysomes, and this contributes to changes in the translational state of specific host mRNAs. We propose that global translational control of the host by eIF4E phosphorylation is a key component of the host-pathogen interaction.
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