Site-Specific Lipidation Enhances IFITM3 Membrane Interactions and Antiviral Activity.
ACS Chem Biol
; 16(5): 844-856, 2021 05 21.
Article
in English
| MEDLINE | ID: covidwho-1457790
ABSTRACT
Interferon-induced transmembrane proteins (IFITMs) are S-palmitoylated proteins in vertebrates that restrict a diverse range of viruses. S-palmitoylated IFITM3 in particular engages incoming virus particles, prevents their cytoplasmic entry, and accelerates their lysosomal clearance by host cells. However, how S-palmitoylation modulates the structure and biophysical characteristics of IFITM3 to promote its antiviral activity remains unclear. To investigate how site-specific S-palmitoylation controls IFITM3 antiviral activity, we employed computational, chemical, and biophysical approaches to demonstrate that site-specific lipidation of cysteine 72 enhances the antiviral activity of IFITM3 by modulating its conformation and interaction with lipid membranes. Collectively, our results demonstrate that site-specific S-palmitoylation of IFITM3 directly alters its biophysical properties and activity in cells to prevent virus infection.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Antiviral Agents
/
Cell Membrane
/
Interferons
/
RNA-Binding Proteins
/
Lipids
/
Membrane Proteins
Limits:
Humans
Language:
English
Journal:
ACS Chem Biol
Year:
2021
Document Type:
Article
Affiliation country:
Acschembio.1c00013
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