Fifty Shades of E<sup>rns</sup>: Innate Immune Evasion by the Viral Endonucleases of All Pestivirus Species
The genus <i>Pestivirus</i>, family <i>Flaviviridae</i>, includes four historically accepted species, i.e., bovine viral diarrhea virus (BVDV)-1 and -2, classical swine fever virus (CSFV), and border disease virus (BDV). A large number of new pestivirus species were identifie...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-01-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/14/2/265 |
| _version_ | 1797475960986009600 |
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| author | Elena de Martin Matthias Schweizer |
| author_facet | Elena de Martin Matthias Schweizer |
| author_sort | Elena de Martin |
| collection | DOAJ |
| description | The genus <i>Pestivirus</i>, family <i>Flaviviridae</i>, includes four historically accepted species, i.e., bovine viral diarrhea virus (BVDV)-1 and -2, classical swine fever virus (CSFV), and border disease virus (BDV). A large number of new pestivirus species were identified in recent years. A common feature of most members is the presence of two unique proteins, N<sup>pro</sup> and E<sup>rns</sup>, that pestiviruses evolved to regulate the host’s innate immune response. In addition to its function as a structural envelope glycoprotein, E<sup>rns</sup> is also released in the extracellular space, where it is endocytosed by neighboring cells. As an endoribonuclease, E<sup>rns</sup> is able to cleave viral ss- and dsRNAs, thus preventing the stimulation of the host’s interferon (IFN) response. Here, we characterize the basic features of soluble E<sup>rns</sup> of a large variety of classified and unassigned pestiviruses that have not yet been described. Its ability to form homodimers, its RNase activity, and the ability to inhibit dsRNA-induced IFN synthesis were investigated. Overall, we found large differences between the various E<sup>rns</sup> proteins that cannot be predicted solely based on their primary amino acid sequences, and that might be the consequence of different virus-host co-evolution histories. This provides valuable information to delineate the structure-function relationship of pestiviral endoribonucleases. |
| first_indexed | 2024-03-09T20:52:14Z |
| format | Article |
| id | doaj.art-1127282c12cc4604bfc879d77c345019 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-09T20:52:14Z |
| publishDate | 2022-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-1127282c12cc4604bfc879d77c3450192023-11-23T22:30:09ZengMDPI AGViruses1999-49152022-01-0114226510.3390/v14020265Fifty Shades of E<sup>rns</sup>: Innate Immune Evasion by the Viral Endonucleases of All Pestivirus SpeciesElena de Martin0Matthias Schweizer1Institute of Virology and Immunology, Länggass-Str. 122, POB, CH-3001 Bern, SwitzerlandInstitute of Virology and Immunology, Länggass-Str. 122, POB, CH-3001 Bern, SwitzerlandThe genus <i>Pestivirus</i>, family <i>Flaviviridae</i>, includes four historically accepted species, i.e., bovine viral diarrhea virus (BVDV)-1 and -2, classical swine fever virus (CSFV), and border disease virus (BDV). A large number of new pestivirus species were identified in recent years. A common feature of most members is the presence of two unique proteins, N<sup>pro</sup> and E<sup>rns</sup>, that pestiviruses evolved to regulate the host’s innate immune response. In addition to its function as a structural envelope glycoprotein, E<sup>rns</sup> is also released in the extracellular space, where it is endocytosed by neighboring cells. As an endoribonuclease, E<sup>rns</sup> is able to cleave viral ss- and dsRNAs, thus preventing the stimulation of the host’s interferon (IFN) response. Here, we characterize the basic features of soluble E<sup>rns</sup> of a large variety of classified and unassigned pestiviruses that have not yet been described. Its ability to form homodimers, its RNase activity, and the ability to inhibit dsRNA-induced IFN synthesis were investigated. Overall, we found large differences between the various E<sup>rns</sup> proteins that cannot be predicted solely based on their primary amino acid sequences, and that might be the consequence of different virus-host co-evolution histories. This provides valuable information to delineate the structure-function relationship of pestiviral endoribonucleases.https://www.mdpi.com/1999-4915/14/2/265pestivirusbovine viral diarrhea virus (BVDV)viral endonucleaseinnate immune evasioninterferon type-Iatypical pestiviruses |
| spellingShingle | Elena de Martin Matthias Schweizer Fifty Shades of E<sup>rns</sup>: Innate Immune Evasion by the Viral Endonucleases of All Pestivirus Species Viruses pestivirus bovine viral diarrhea virus (BVDV) viral endonuclease innate immune evasion interferon type-I atypical pestiviruses |
| title | Fifty Shades of E<sup>rns</sup>: Innate Immune Evasion by the Viral Endonucleases of All Pestivirus Species |
| title_full | Fifty Shades of E<sup>rns</sup>: Innate Immune Evasion by the Viral Endonucleases of All Pestivirus Species |
| title_fullStr | Fifty Shades of E<sup>rns</sup>: Innate Immune Evasion by the Viral Endonucleases of All Pestivirus Species |
| title_full_unstemmed | Fifty Shades of E<sup>rns</sup>: Innate Immune Evasion by the Viral Endonucleases of All Pestivirus Species |
| title_short | Fifty Shades of E<sup>rns</sup>: Innate Immune Evasion by the Viral Endonucleases of All Pestivirus Species |
| title_sort | fifty shades of e sup rns sup innate immune evasion by the viral endonucleases of all pestivirus species |
| topic | pestivirus bovine viral diarrhea virus (BVDV) viral endonuclease innate immune evasion interferon type-I atypical pestiviruses |
| url | https://www.mdpi.com/1999-4915/14/2/265 |
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