☆ 4.7 Review

Host antiviral factors hijack furin to block SARS-CoV-2, ebola virus, and HIV-1 glycoproteins cleavage

EMERGING MICROBES & INFECTIONS (2023)

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Summary: This article specifically discusses the effects of the furin cleavage site on the spike protein of SARS-CoV-2, highlighting its impact on viral replication, pathogenesis, host immune responses, and vaccination. It offers novel insights into the current COVID-19 pandemic.

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Summary: Loss of the furin cleavage motif in SARS-CoV-2 spike protein reduces its virulence and transmission. Alpha-soluble NSF attachment protein (alpha-SNAP), besides its role in vesicle trafficking, inhibits the cleavage of SARS-CoV-2 spike protein, demonstrating its potential as a therapeutic target for COVID-19. The study also reveals that alpha-SNAP is an interferon-upregulated furin inhibitor that plays an important role in host defense against furin-dependent virus infection.

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Summary: MARCH8 is an antiviral factor that can inhibit viral envelope glycoproteins by recognizing their cytoplasmic lysine residues, resulting in lysosomal degradation. This study reveals the broad-spectrum inhibitory activity of MARCH8 against various viral envelope glycoproteins.

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SARS-CoV-2 Variants of Concern Hijack IFITM2 for Efficient Replication in Human Lung Cells

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