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Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation
Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation
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Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation
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Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation
Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation

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Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation
Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation
Journal Article

Interferon-inducible guanylate-binding protein 5 inhibits replication of multiple viruses by binding to the oligosaccharyltransferase complex and inhibiting glycoprotein maturation

2025
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Overview
Viral infection induces production of type I interferons and expression of interferon-stimulated genes (ISGs) that play key roles in inhibiting viral infection. We found that the interferon-stimulated gene GBP5 is induced by SARS-CoV-2 infection in vitro and in vivo . GBP5 inhibits N-glycosylation of key proteins in multiple viruses, including SARS-CoV-2. Importantly, pharmacological inhibition of oligosaccharyltransferase (OST) complex blocks host cell infection by SARS-CoV-2, variants of concern, HIV-1, and IAV, indicating future translational application of our findings.