Gene Name | PRDX1 |
HF Protein Name | Peroxiredoxin-1 |
HF Function | Required for efficient transcription and replication of Measles Virus |
Uniprot ID | Q06830 |
Protein Sequence | View Fasta Sequence |
NCBI Gene ID | 5052 |
Host Factor (HF) Name in Paper | Prdx1 |
Gene synonyms | PAGA PAGB TDPX2 |
Ensemble Gene ID | ENSG00000117450 |
Ensemble Transcript | ENST00000262746;ENST00000319248 |
KEGG ID | Go to KEGG Database |
Gene Ontology ID(s) | GO:0001501, GO:0001895, GO:0003723, GO:0004601, GO:0005615, GO:0005634, GO:0005737, GO:0005739, GO:0005829, GO:0008283, GO:0008379, GO:0019430, GO:0030101, GO:0032872, GO:0034101, GO:0034599, GO:0042267, GO:0042345, GO:0042470, GO:0042744, GO:0042802, GO:0043209, GO:0045296, GO:0045454, GO:0070062, |
MINT ID | Q06830 |
STRING | Click to see interaction map |
GWAS Analysis | Click to see gwas analysis |
OMIM ID | 176763 |
PANTHER ID | N.A. |
PDB ID(s) | 2RII, 3HY2, 4XCS, |
pfam ID | PF10417, PF00578, |
Drug Bank ID | N.A., |
ChEMBL ID | CHEMBL5315 |
Organism | Homo sapiens (Human) |
Virus Name | Measles Virus |
Virus Short Name | MeV |
Order | Mononegavirales |
Virus Family | Paramyxoviridae |
Virus Subfamily | N.A. |
Genus | Morbilivirus |
Species | Measles morbillivirus |
Host | Human, dog, cattle |
Cell Tropism | N.A. |
Associated Disease | Fever, rash |
Mode of Transmission | Respiratory |
VIPR DB link | http://www.viprbrc.org/brc/vipr_allSpecies_search.do?method=SubmitForm&decorator=paramyxo |
ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/negative-sense-rna-viruses-2011/w/negrna_viruses/199/paramyxoviridae |
Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Paramyxoviridae |
Paper Title | Peroxiredoxin 1 is required for efficient transcription and replication of measles virus |
Author's Name | Akira Watanabe, Misako Yoneda, Fusako Ikeda, Akihiro Sugai, Hiroki Sato and Chieko Kai |
Journal Name | Journal Of Virology |
Pubmed ID | 21159870 |
Abstract | Measles is a highly contagious human disease caused by the measles virus (MeV). In this study, by proteomic analysis, we identified peroxiredoxin 1 (Prdx1) as a host factor that binds to the C-terminal region of the nucleoprotein (N N(TAIL)) of MeV. Glutathione S-transferase (GST) pulldown experiments showed that the Prdx1-binding site overlapped with the MeV phosphoprotein (P)-binding site on N(TAIL) and that Prdx1 competed for the binding to N(TAIL) with the P protein, which is a component of RNA-dependent RNA polymerase (RdRp). Furthermore, RNA interference for Prdx1 resulted in a significant reduction in MeV growth in HEK293-SLAM cells. A minigenome assay indicated that Prdx1 suppression affected the viral RNA transcription and/or replication step. Relative quantification of viral RNA by real-time PCR (RT-PCR) showed that Prdx1 suppression not only reduced viral RNA transcription and replication but also enhanced polar attenuation in viral mRNA transcription. Surface plasmon resonance analysis showed that the binding affinity of Prdx1 to MeV-N was 40-fold lower than that of MeV-P to MeV-N, which suggested that Prdx1 might be involved in the early stage of MeV infection, when the expression level of Prdx1 was much higher than that of MeV-P. Since Prdx1 was expressed abundantly and constitutively in various cells, the results in this study indicate that Prdx1 is one of the inherent host factors implicated in MeV RNA synthesis. |
Used Model | HEK293-SLAM cells |
DOI | 10.1128/JVI.01796-10 |