Antiviral mechanisms of guanylate-binding protein 5: versatile inhibition of multiple viral glycoproteins.
| Autor: | Sauter D; Institute for Medical Virology and Epidemiology of Viral Diseases, University Hospital Tübingen, Tübingen, Germany., Kirchhoff F; Institute of Molecular Virology, Ulm University Medical Center, Ulm, Germany. |
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| Jazyk: | angličtina |
| Zdroj: | MBio [mBio] 2024 Nov 13; Vol. 15 (11), pp. e0237424. Date of Electronic Publication: 2024 Oct 15. |
| DOI: | 10.1128/mbio.02374-24 |
| Abstrakt: | Guanylate-binding proteins (GBPs) are interferon-inducible cellular factors known to inhibit a wide variety of pathogens. Humans encode seven GBPs that have functionally diversified to provide broad protection against a variety of bacteria, protozoa, and viruses. Here, we discuss recent data on the mechanisms underlying the broad antiviral activity of GBP5 (H. Veler, C. M. Lun, A. A. Waheed, and E. O. Freed, mBio e02086-24, 2024, https://doi.org/10.1128/mbio.02086-24) and place them in the context of previous studies on the ability of this antiviral factor to impair the function of numerous viral envelope (Env) glycoproteins. We focus on the effects of GBP5 on the glycosylation, proteolytic processing, and anterograde transport of Env and discuss mechanistic interdependencies of these maturation steps. Understanding the induction and action of broadly acting immune factors, such as GBP5, may help develop effective immune-based strategies against numerous pathogens. Competing Interests: The authors declare no conflict of interest. |
| Databáze: | MEDLINE |
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