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Respiratory syncytial virus induces host RNA stress granules to facilitate viral replication.
Lindquist ME, Lifland AW, Utley TJ, Santangelo PJ, Crowe JE
(2010) J Virol 84: 12274-84
MeSH Terms: Antigens, Surface, Blotting, Western, Carrier Proteins, Cell Line, Cytoplasmic Granules, DNA Helicases, ELAV Proteins, ELAV-Like Protein 1, Epithelial Cells, Humans, Poly-ADP-Ribose Binding Proteins, RNA Helicases, RNA Interference, RNA Recognition Motif Proteins, RNA, Messenger, RNA-Binding Proteins, Respiratory Syncytial Virus Infections, Respiratory Syncytial Viruses, Reverse Transcriptase Polymerase Chain Reaction, Stress, Physiological, Virus Replication
Show Abstract · Added August 6, 2012
Mammalian cell cytoplasmic RNA stress granules are induced during various conditions of stress and are strongly associated with regulation of host mRNA translation. Several viruses induce stress granules during the course of infection, but the exact function of these structures during virus replication is not well understood. In this study, we showed that respiratory syncytial virus (RSV) induced host stress granules in epithelial cells during the course of infection. We also showed that stress granules are distinct from cytoplasmic viral inclusion bodies and that the RNA binding protein HuR, normally found in stress granules, also localized to viral inclusion bodies during infection. Interestingly, we demonstrated that infected cells containing stress granules also contained more RSV protein than infected cells that did not form inclusion bodies. To address the role of stress granule formation in RSV infection, we generated a stable epithelial cell line with reduced expression of the Ras-GAP SH3 domain-binding protein (G3BP) that displayed an inhibited stress granule response. Surprisingly, RSV replication was impaired in these cells compared to its replication in cells with intact G3BP expression. In contrast, knockdown of HuR by RNA interference did not affect stress granule formation or RSV replication. Finally, using RNA probes specific for RSV genomic RNA, we found that viral RNA predominantly localized to viral inclusion bodies but a small percentage also interacted with stress granules during infection. These results suggest that RSV induces a host stress granule response and preferentially replicates in host cells that have committed to a stress response.
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HuR/methyl-HuR and AUF1 regulate the MAT expressed during liver proliferation, differentiation, and carcinogenesis.
Vázquez-Chantada M, Fernández-Ramos D, Embade N, Martínez-Lopez N, Varela-Rey M, Woodhoo A, Luka Z, Wagner C, Anglim PP, Finnell RH, Caballería J, Laird-Offringa IA, Gorospe M, Lu SC, Mato JM, Martínez-Chantar ML
(2010) Gastroenterology 138: 1943-53
MeSH Terms: 3' Untranslated Regions, Animals, Antigens, Surface, Binding Sites, Cell Differentiation, Cell Proliferation, Cell Transformation, Neoplastic, Cells, Cultured, ELAV Proteins, ELAV-Like Protein 1, Gene Expression Regulation, Developmental, Gene Expression Regulation, Enzymologic, Gestational Age, Glycine N-Methyltransferase, Half-Life, Hepatocytes, Heterogeneous-Nuclear Ribonucleoprotein D, Humans, Liver Neoplasms, Male, Methionine Adenosyltransferase, Methylation, Mice, Mice, Inbred C57BL, RNA Interference, RNA Processing, Post-Transcriptional, RNA Stability, RNA, Messenger, RNA-Binding Proteins, Rats, Rats, Wistar, S-Adenosylmethionine, Signal Transduction, Transfection
Show Abstract · Added January 20, 2015
BACKGROUND & AIMS - Hepatic de-differentiation, liver development, and malignant transformation are processes in which the levels of hepatic S-adenosylmethionine are tightly regulated by 2 genes: methionine adenosyltransferase 1A (MAT1A) and methionine adenosyltransferase 2A (MAT2A). MAT1A is expressed in the adult liver, whereas MAT2A expression primarily is extrahepatic and is associated strongly with liver proliferation. The mechanisms that regulate these expression patterns are not completely understood.
METHODS - In silico analysis of the 3' untranslated region of MAT1A and MAT2A revealed putative binding sites for the RNA-binding proteins AU-rich RNA binding factor 1 (AUF1) and HuR, respectively. We investigated the posttranscriptional regulation of MAT1A and MAT2A by AUF1, HuR, and methyl-HuR in the aforementioned biological processes.
RESULTS - During hepatic de-differentiation, the switch between MAT1A and MAT2A coincided with an increase in HuR and AUF1 expression. S-adenosylmethionine treatment altered this homeostasis by shifting the balance of AUF1 and methyl-HuR/HuR, which was identified as an inhibitor of MAT2A messenger RNA (mRNA) stability. We also observed a similar temporal distribution and a functional link between HuR, methyl-HuR, AUF1, and MAT1A and MAT2A during fetal liver development. Immunofluorescent analysis revealed increased levels of HuR and AUF1, and a decrease in methyl-HuR levels in human livers with hepatocellular carcinoma (HCC).
CONCLUSIONS - Our data strongly support a role for AUF1 and HuR/methyl-HuR in liver de-differentiation, development, and human HCC progression through the posttranslational regulation of MAT1A and MAT2A mRNAs.
Copyright 2010 AGA Institute. Published by Elsevier Inc. All rights reserved.
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34 MeSH Terms