Interferon-induced transmembrane protein 3 (IFITM3) and its antiviral activity

ElsevierVolume 77, December 2022, 102467Current Opinion in Structural BiologyAbstract

Infections caused by enveloped viruses require fusion with cellular membranes for viral genome entry. Viral entry occurs following an interaction of viral and cellular membranes allowing the formation of fusion pores, by which the virus accesses the cytoplasm. Here, we focus on interferon-induced transmembrane protein 3 (IFITM3) and its antiviral activity. IFITM3 is predicted to block or stall viral fusion at an intermediate state, causing viral propagation to fail. After introducing IFITM3, we describe the generalized lipid membrane fusion pathway and how it can be stalled, particularly with respect to IFITM3, and current questions regarding IFITM3's topology, with specific emphasis on IFITM3's amphipathic α-helix (AAH) 59V-68M, which is necessary for the antiviral activity. We report new hydrophobicity and hydrophobic moment calculations for this peptide and a variety of active site peptides from known membrane-remodeling proteins. Finally, we discuss the effects of posttranslational modifications and localization, how IFITM3's AAH may block viral fusion, and possible ramifications of membrane composition.

Keywords

Influenza

HIV

Innate immunity

Interferon

Amphipathic Alpha Helix

Hydrophobicity

Hydrophobic Moment

Membrane Fusion

Enveloped Virus

View full text

© 2022 Published by Elsevier Ltd.

留言 (0)

沒有登入
gif