IFITM proteins promote SARS-CoV-2 infection and are targets for virus inhibition in vitro.

Interferon-induced transmembrane proteins (IFITMs 1, 2 and 3) can restrict viral pathogens, but pro- and anti-viral activities have been reported for coronaviruses. Here, we show that artificial overexpression of IFITMs blocks SARS-CoV-2 infection. However, endogenous IFITM expression supports efficient infection of SARS-CoV-2 in human lung cells. Our results indicate that ...
the SARS-CoV-2 Spike protein interacts with IFITMs and hijacks them for efficient viral infection. IFITM proteins were expressed and further induced by interferons in human lung, gut, heart and brain cells. IFITM-derived peptides and targeting antibodies inhibit SARS-CoV-2 entry and replication in human lung cells, cardiomyocytes and gut organoids. Our results show that IFITM proteins are cofactors for efficient SARS-CoV-2 infection of human cell types representing in vivo targets for viral transmission, dissemination and pathogenesis and are potential targets for therapeutic approaches.
Mesh Terms:
Amino Acid Sequence, Angiotensin-Converting Enzyme 2, Antibodies, Neutralizing, Antigens, Differentiation, Binding Sites, COVID-19, Gene Expression Regulation, Host-Pathogen Interactions, Humans, Interferon-beta, Membrane Proteins, Protein Binding, Protein Interaction Domains and Motifs, RNA, Small Interfering, RNA-Binding Proteins, SARS-CoV-2, Sequence Alignment, Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus, Virus Attachment
Nat Commun
Date: Dec. 28, 2020
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