Coxsackievirus B3 2A protease promotes encephalomyocarditis virus replication

To determine whether 2A protease of the enterovirus genus with type I internal ribosome entry site (IRES) effect on the viral replication of type II IRES, coxsackievirus B3(CVB3)-encoded protease 2A and encephalomyocarditis virus (EMCV) IRES (Type II)-dependent or cap-dependent report gene were tran...

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Bibliographic Details
Published in:Virus research 2015-10, Vol.208, p.22-29
Main Authors: Song, Qin-Qin, Lu, Ming-Zhi, Song, Juan, Chi, Miao-Miao, Sheng, Lin-Jun, Yu, Jie, Luo, Xiao-Nuan, Zhang, Lu, Yao, Hai-Lan, Han, Jun
Format: Article
Language:English
Subjects:
2A protease
Amino Acid Motifs
Cardiovirus Infections - virology
Coxsackievirus B3
Cysteine Endopeptidases - chemistry
Cysteine Endopeptidases - genetics
Cysteine Endopeptidases - metabolism
EMCV
Encephalomyocarditis virus
Encephalomyocarditis virus - genetics
Encephalomyocarditis virus - physiology
Enterovirus
Enterovirus B, Human - enzymology
Enterovirus B, Human - genetics
Enterovirus Infections - virology
Humans
IRES
Protein Biosynthesis
Protein translation
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - metabolism
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Summary:To determine whether 2A protease of the enterovirus genus with type I internal ribosome entry site (IRES) effect on the viral replication of type II IRES, coxsackievirus B3(CVB3)-encoded protease 2A and encephalomyocarditis virus (EMCV) IRES (Type II)-dependent or cap-dependent report gene were transiently co-expressed in eukaryotic cells. We found that CVB3 2A protease not only inhibited translation of cap-dependent reporter genes through the cleavage of eIF4GI, but also conferred high EMCV IRES-dependent translation ability and promoted EMCV replication. Moreover, deletions of short motif (aa13–18 RVVNRH, aa65–70 KNKHYP, or aa88–93 PRRYQSH) resembling the nuclear localization signals (NLS) or COOH-terminal acidic amino acid motif (aa133–147 DIRDLLWLEDDAMEQ) of CVB3 2A protease decreased both its EMCV IRES-dependent translation efficiency and destroy its cleavage on eukaryotic initiation factor 4G (eIF4G) I. Our results may provide better understanding into more effective interventions and treatments for co-infection of viral diseases.
ISSN:0168-1702
1872-7492
DOI:10.1016/j.virusres.2015.05.020