Zika virus prM protein contains cholesterol binding motifs required for virus entry and assembly.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
13 11 2023
13 11 2023
Historique:
received:
02
03
2023
accepted:
25
10
2023
medline:
15
11
2023
pubmed:
14
11
2023
entrez:
13
11
2023
Statut:
epublish
Résumé
For successful infection of host cells and virion production, enveloped viruses, including Zika virus (ZIKV), extensively rely on cellular lipids. However, how virus protein-lipid interactions contribute to the viral life cycle remains unclear. Here, we employ a chemo-proteomics approach with a bifunctional cholesterol probe and show that cholesterol is closely associated with the ZIKV structural protein prM. Bioinformatic analyses, reverse genetics alongside with photoaffinity labeling assays, and atomistic molecular dynamics simulations identified two functional cholesterol binding motifs within the prM transmembrane domain. Loss of prM-cholesterol association has a bipartite effect reducing ZIKV entry and leading to assembly defects. We propose a model in which membrane-resident M facilitates cholesterol-supported lipid exchange during endosomal entry and, together with cholesterol, creates a platform promoting virion assembly. In summary, we identify a bifunctional role of prM in the ZIKV life cycle by mediating viral entry and virus assembly in a cholesterol-dependent manner.
Identifiants
pubmed: 37957166
doi: 10.1038/s41467-023-42985-x
pii: 10.1038/s41467-023-42985-x
pmc: PMC10643666
doi:
Substances chimiques
Viral Proteins
0
Lipids
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7344Informations de copyright
© 2023. The Author(s).
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