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Tytuł:
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ISG15 overexpression compensates the defect of Crimean-Congo hemorrhagic fever virus polymerase bearing a protease-inactive ovarian tumor domain.
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Autorzy:
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Devignot S; Institute for Virology, FB10-Veterinary Medicine, Justus-Liebig University, Giessen, Germany.
Kromer T; Faculty of Health, Safety, Society, Furtwangen University, Furtwangen, Germany.
Mirazimi A; Public Health Agency of Sweden, Solna, Sweden.; National Veterinary Institute, Solna, Sweden.; Karolinska Institute, Stockholm, Sweden.
Weber F; Institute for Virology, FB10-Veterinary Medicine, Justus-Liebig University, Giessen, Germany.
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Źródło:
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PLoS neglected tropical diseases [PLoS Negl Trop Dis] 2020 Sep 15; Vol. 14 (9), pp. e0008610. Date of Electronic Publication: 2020 Sep 15 (Print Publication: 2020).
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Original Publication: San Francisco, CA : Public Library of Science
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MeSH Terms:
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Cytokines/*genetics
DNA-Directed RNA Polymerases/*genetics
Hemorrhagic Fever Virus, Crimean-Congo/*genetics
Hemorrhagic Fever Virus, Crimean-Congo/*immunology
Peptide Hydrolases/*genetics
Ubiquitins/*genetics
A549 Cells ; Animals ; Cell Line, Tumor ; Chlorocebus aethiops ; Cytokines/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Hemorrhagic Fever, Crimean/pathology ; Humans ; Interferon Type I/immunology ; Protein Domains/genetics ; Protein Processing, Post-Translational/genetics ; Ubiquitins/metabolism ; Vero Cells
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References:
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Substance Nomenclature:
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0 (Cytokines)
0 (Interferon Type I)
0 (Ubiquitins)
60267-61-0 (ISG15 protein, human)
EC 2.7.7.6 (DNA-Directed RNA Polymerases)
EC 3.4.- (Peptide Hydrolases)
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Entry Date(s):
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Date Created: 20200915 Date Completed: 20201028 Latest Revision: 20201028
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Update Code:
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20240104
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PubMed Central ID:
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PMC7518590
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DOI:
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10.1371/journal.pntd.0008610
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PMID:
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32931521
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Crimean-Congo Hemorrhagic Fever virus (CCHFV; family Nairoviridae) is an extremely pathogenic member of the Bunyavirales order. Previous studies have shown that the N-terminal domain of the CCHFV polymerase (L) contains an ovarian tumor-type protease (OTU) domain with the capability to remove both ubiquitin and ISG15 molecules from proteins. The approximately 200 amino acids-long OTU domain, if ectopically expressed, can interfere with both the induction of antiviral type I interferons (IFN) as well as the IFN-stimulated signaling. A OTU protease mutant (C40A), by contrast, was inactive in that respect. However, the effect of the OTU protease activity in the context of the full-length L protein (approximately 4000 amino acids) is only poorly characterized, and recombinant CCHFV with the C40A mutation could not be rescued. Here, we employed transcriptionally active virus-like particles (tc-VLPs) to investigate the interaction between the L-embedded OTU protease and the IFN system. Our data show a cis requirement of the OTU protease for optimal CCHFV polymerase activity in human HuH-7 cells. The L-embedded OTU did not influence IFN signaling, the sensitivity to IFN, or IFN induction. Moreover, the attenuation of OTU C40A-mutated L could not be relieved by inactivating the IFN response, but after overexpression of conjugation-competent ISG15 the polymerase activity recovered to wild-type levels. Consequently, ISG15 was used to produce OTU-deficient tc-VLPs, a potential vaccine candidate. Our data thus indicate that in the context of full-length L the OTU domain is important for the regulation of CCHFV polymerase by ISG15.
Competing Interests: The authors have declared that no competing interests exist.
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