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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. | LitMetric

Interferon-Inducible Guanylate-Binding Protein 5 Inhibits Replication of Multiple Viruses by Binding to the Oligosaccharyltransferase Complex and Inhibiting Glycoprotein Maturation.

bioRxiv

Division of Genetics, Department of Pediatrics, Program in Immunology, Bioinformatics and Systems Biology Program, Institute for Genomic Medicine, UCSD Center for AIDS Research, University of California San Diego, 9500 Gilman Drive MC 0762, La Jolla, California 92093, USA.

Published: May 2024

AI Article Synopsis

  • Viral infections trigger the production of type I interferons and interferon-stimulated genes (ISGs) that help combat these infections.
  • The ISG guanylate-binding protein 5 (GBP5) interferes with N-linked glycosylation of viral proteins, specifically blocking the spike protein of SARS-CoV-2 by binding to host cellular components.
  • Pharmacological inhibition of the glycosylation process with NGI-1 shows potential as an effective antiviral strategy against multiple viruses by preventing the formation of infectious particles.

Article Abstract

Viral infection induces production of type I interferons and expression of interferon-stimulated genes (ISGs) that play key roles in inhibiting viral infection. Here, we show that the ISG guanylate-binding protein 5 (GBP5) inhibits N-linked glycosylation of key proteins in multiple viruses, including SARS-CoV-2 spike protein. GBP5 binds to accessory subunits of the host oligosaccharyltransferase (OST) complex and blocks its interaction with the spike protein, which results in misfolding and retention of spike protein in the endoplasmic reticulum likely due to decreased -glycan transfer, and reduces the assembly and release of infectious virions. Consistent with these observations, pharmacological inhibition of the OST complex with NGI-1 potently inhibits glycosylation of other viral proteins, including MERS-CoV spike protein, HIV-1 gp160, and IAV hemagglutinin, and prevents the production of infectious virions. Our results identify a novel strategy by which ISGs restrict virus infection and provide a rationale for targeting glycosylation as a broad antiviral therapeutic strategy.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11092618PMC
http://dx.doi.org/10.1101/2024.05.01.591800DOI Listing

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