| First Author | Hernáez B | Year | 2018 |
| Journal | Nat Commun | Volume | 9 |
| Issue | 1 | Pages | 5440 |
| PubMed ID | 30575728 | Mgi Jnum | J:270645 |
| Mgi Id | MGI:6277531 | Doi | 10.1038/s41467-018-07772-z |
| Citation | Hernaez B, et al. (2018) A virus-encoded type I interferon decoy receptor enables evasion of host immunity through cell-surface binding. Nat Commun 9(1):5440 |
| abstractText | Soluble cytokine decoy receptors are potent immune modulatory reagents with therapeutic applications. Some virus-encoded secreted cytokine receptors interact with glycosaminoglycans expressed at the cell surface, but the biological significance of this activity in vivo is poorly understood. Here, we show the type I interferon binding protein (IFNalpha/betaBP) encoded by vaccinia and ectromelia viruses requires of this cell binding activity to confer full virulence to these viruses and to retain immunomodulatory activity. Expression of a variant form of the IFNalpha/betaBP that inhibits IFN activity, but does not interact with cell surface glycosaminoglycans, results in highly attenuated viruses with a virulence similar to that of the IFNalpha/betaBP deletion mutant viruses. Transcriptomics analysis and infection of IFN receptor-deficient mice confirmed that the control of IFN activity is the main function of the IFNalpha/betaBP in vivo. We propose that retention of secreted cytokine receptors at the cell surface may largely enhance their immunomodulatory activity. |
