Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interaction with 3' ends of Japanese encephalitis virus RNA and colocalization with the viral NS5 protein

Replication of the Japanese encephalitis virus (JEV) genome depends on host factors for successfully completing their life cycles; to do this, host factors have been recruited and/or relocated to the site of viral replication. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a cellular metabolic pr...

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Bibliographic Details
Published in:Journal of biomedical science 2009-04, Vol.16 (1), p.40-40, Article 40
Main Authors: Yang, Shang-Hua, Liu, Mei-Lan, Tien, Chih-Feng, Chou, Shih-Jie, Chang, Ruey-Yi
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Cells, Cultured
Cricetinae
Encephalitis Virus, Japanese - genetics
Encephalitis Virus, Japanese - metabolism
Enzymes
Fluorescent Antibody Technique
Genomes
Glyceraldehyde-3-Phosphate Dehydrogenases - analysis
Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism
Health aspects
Humans
Japanese encephalitis
Monosaccharides
Phosphates
RNA
RNA Replicase - metabolism
RNA, Viral - metabolism
Sugars
Viral Nonstructural Proteins - metabolism
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Summary:Replication of the Japanese encephalitis virus (JEV) genome depends on host factors for successfully completing their life cycles; to do this, host factors have been recruited and/or relocated to the site of viral replication. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a cellular metabolic protein, was found to colocalize with viral RNA-dependent RNA polymerase (NS5) in JEV-infected cells. Subcellular fractionation further indicated that GAPDH remained relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection (hpi) and decreasing at 36 hpi in the nuclear fraction of infected cells. In contrast, the redistribution patterns of GAPDH were not observed in the uninfected cells. Co-immunoprecipitation of GAPDH and JEV NS5 protein revealed no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of JEV by electrophoretic mobility shift assays. Accordingly, GAPDH binds to the minus strand more efficiently than to the plus strand of JEV RNAs. This study highlights the findings that infection of JEV changes subcellular localization of GAPDH suggesting that this metabolic enzyme may play a role in JEV replication.
ISSN:1423-0127
1021-7770
1423-0127
DOI:10.1186/1423-0127-16-40