Analysis of the Zika and Japanese Encephalitis Virus NS5 Interactomes.
Animals
Dengue
/ genetics
Dengue Virus
/ genetics
Encephalitis Virus, Japanese
/ genetics
Encephalitis, Arbovirus
/ genetics
HEK293 Cells
Host-Pathogen Interactions
/ genetics
Humans
Mass Spectrometry
/ methods
Protein Interaction Maps
/ genetics
Receptors, Steroid
/ genetics
Viral Nonstructural Proteins
/ genetics
Virus Replication
/ genetics
Zika Virus
/ genetics
Zika Virus Infection
/ genetics
Japanese encephalitis virus
NS5
Zika virus
flavivirus
nonstructural protein 5
Journal
Journal of proteome research
ISSN: 1535-3907
Titre abrégé: J Proteome Res
Pays: United States
ID NLM: 101128775
Informations de publication
Date de publication:
02 08 2019
02 08 2019
Historique:
pubmed:
15
6
2019
medline:
16
7
2020
entrez:
15
6
2019
Statut:
ppublish
Résumé
Mosquito-borne flaviviruses, including dengue virus (DENV), Japanese encephalitis virus (JEV), and Zika virus (ZIKV), are major human pathogens. Among the flaviviral proteins, the nonstructural protein 5 (NS5) is the largest, most conserved, and major enzymatic component of the viral replication complex. Disruption of the common key NS5-host protein-protein interactions critical for viral replication could aid in the development of broad-spectrum antiflaviviral therapeutics. Hundreds of NS5 interactors have been identified, but these are mostly DENV-NS5 interactors. To this end, we sought to investigate the JEV- and ZIKV-NS5 interactomes using EGFP immunoprecipitation with label-free quantitative mass spectrometry analysis. We report here a total of 137 NS5 interactors with a significant enrichment of spliceosomal and spliceosomal-associated proteins. The transcription complex Paf1C and phosphatase 6 were identified as common NS5-associated complexes. PAF1 was shown to play opposite roles in JEV and ZIKV infections. Additionally, we validated several NS5 targets and proposed their possible roles in infection. These include lipid-shuttling proteins OSBPL9 and OSBPL11, component of RNAP3 transcription factor TFIIIC, minichromosome maintenance, and cochaperone PAQosome. Mining this data set, our study expands the current interaction landscape of NS5 and uncovers several NS5 targets that are new to flavivirus biology.
Identifiants
pubmed: 31199156
doi: 10.1021/acs.jproteome.9b00318
doi:
Substances chimiques
NS5 protein, flavivirus
0
Receptors, Steroid
0
Viral Nonstructural Proteins
0
oxysterol binding protein
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM