The Cytomegalovirus M35 Protein Directly Binds to the Interferon-β Enhancer and Modulates Transcription of
DNA-binding protein
IRF3
IRF3-dependent genes
M35
MCMV
PRR signalling
SLAM sequencing (SLAM-seq)
U14
cytomegalovirus
herpesvirus
immune evasion
innate immunity
interferon-stimulated genes (ISG)
pp85 protein superfamily
type I interferon (IFN) response
Journal
Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724
Informations de publication
Date de publication:
29 06 2023
29 06 2023
Historique:
medline:
3
7
2023
pubmed:
8
6
2023
entrez:
8
6
2023
Statut:
ppublish
Résumé
Induction of type I interferon (IFN) gene expression is among the first lines of cellular defense a virus encounters during primary infection. We previously identified the tegument protein M35 of murine cytomegalovirus (MCMV) as an essential antagonist of this antiviral system, showing that M35 interferes with type I IFN induction downstream of pattern-recognition receptor (PRR) activation. Here, we report structural and mechanistic details of M35's function. Determination of M35's crystal structure combined with reverse genetics revealed that homodimerization is a key feature for M35's immunomodulatory activity. In electrophoretic mobility shift assays (EMSAs), purified M35 protein specifically bound to the regulatory DNA element that governs transcription of the first type I IFN gene induced in nonimmune cells,
Identifiants
pubmed: 37289084
doi: 10.1128/jvi.00400-23
pmc: PMC10308904
doi:
Substances chimiques
DNA
9007-49-2
Interferon Regulatory Factor-3
0
Interferon Type I
0
Interferon-beta
77238-31-4
Viral Matrix Proteins
0
Irf3 protein, mouse
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0040023Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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