Site-Specific Lipidation Enhances IFITM3 Membrane Interactions and Antiviral Activity.
Site-Specific Lipidation Enhances IFITM3 Membrane Interactions and Antiviral Activity.
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位点特异性脂质化增强 IFITM3 膜相互作用和抗病毒活性
DOI:
10.1021/acschembio.1c00013
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发表时间:
2021-05-21
影响因子:
4
通讯作者:
Hang, Howard C.
中科院分区:
文献类型:
--
作者:
Garst, Emma H.;Lee, Hwayoung;Das, Tandrila;Bhattacharya, Shibani;Percher, Avital;Wiewiora, Rafal;Witte, Isaac P.;Li, Yumeng;Peng, Tao;Im, Wonpil;Hang, Howard C.
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.
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