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Publications (10 of 21) Show all publications
Willekens, S. M. A., Morini, F., Mediavilla, T., Nilsson, E., Orädd, G., Hahn, M., . . . Marcellino, D. (2024). An MR-based brain template and atlas for optical projection tomography and light sheet fluorescence microscopy in neuroscience. Frontiers in Neuroscience, 18, Article ID 1328815.
Open this publication in new window or tab >>An MR-based brain template and atlas for optical projection tomography and light sheet fluorescence microscopy in neuroscience
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2024 (English)In: Frontiers in Neuroscience, ISSN 1662-4548, E-ISSN 1662-453X, Vol. 18, article id 1328815Article in journal (Refereed) Published
Abstract [en]

Introduction: Optical Projection Tomography (OPT) and light sheet fluorescence microscopy (LSFM) are high resolution optical imaging techniques, ideally suited for ex vivo 3D whole mouse brain imaging. Although they exhibit high specificity for their targets, the anatomical detail provided by tissue autofluorescence remains limited.

Methods: T1-weighted images were acquired from 19 BABB or DBE cleared brains to create an MR template using serial longitudinal registration. Afterwards, fluorescent OPT and LSFM images were coregistered/normalized to the MR template to create fusion images.

Results: Volumetric calculations revealed a significant difference between BABB and DBE cleared brains, leading to develop two optimized templates, with associated tissue priors and brain atlas, for BABB (OCUM) and DBE (iOCUM). By creating fusion images, we identified virus infected brain regions, mapped dopamine transporter and translocator protein expression, and traced innervation from the eye along the optic tract to the thalamus and superior colliculus using cholera toxin B. Fusion images allowed for precise anatomical identification of fluorescent signal in the detailed anatomical context provided by MR.

Discussion: The possibility to anatomically map fluorescent signals on magnetic resonance (MR) images, widely used in clinical and preclinical neuroscience, would greatly benefit applications of optical imaging of mouse brain. These specific MR templates for cleared brains enable a broad range of neuroscientific applications integrating 3D optical brain imaging.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2024
Keywords
brain template, LSFM, mesoscopic imaging, MRI, neuroimaging, OPT
National Category
Neurosciences Radiology, Nuclear Medicine and Medical Imaging
Identifiers
urn:nbn:se:umu:diva-223641 (URN)10.3389/fnins.2024.1328815 (DOI)001198866200001 ()38601090 (PubMedID)2-s2.0-85189910322 (Scopus ID)
Funder
The Kempe FoundationsSwedish Research Council, 2020-06224Swedish Research Council, 2018-05851Swedish Research Council, 2020-02300Novo Nordisk FoundationFamiljen Erling-Perssons Stiftelse
Available from: 2024-04-24 Created: 2024-04-24 Last updated: 2024-04-24Bibliographically approved
Garvanska, D. H., Alvarado, R. E., Mundt, F. O., Lindquist, R., Duel, J. K., Coscia, F., . . . Nilsson, J. (2024). The NSP3 protein of SARS-CoV-2 binds fragile X mental retardation proteins to disrupt UBAP2L interactions. EMBO Reports, 25(2), 902-926
Open this publication in new window or tab >>The NSP3 protein of SARS-CoV-2 binds fragile X mental retardation proteins to disrupt UBAP2L interactions
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2024 (English)In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 25, no 2, p. 902-926Article in journal (Refereed) Published
Abstract [en]

Viruses interact with numerous host factors to facilitate viral replication and to dampen antiviral defense mechanisms. We currently have a limited mechanistic understanding of how SARS-CoV-2 binds host factors and the functional role of these interactions. Here, we uncover a novel interaction between the viral NSP3 protein and the fragile X mental retardation proteins (FMRPs: FMR1, FXR1-2). SARS-CoV-2 NSP3 mutant viruses preventing FMRP binding have attenuated replication in vitro and reduced levels of viral antigen in lungs during the early stages of infection. We show that a unique peptide motif in NSP3 binds directly to the two central KH domains of FMRPs and that this interaction is disrupted by the I304N mutation found in a patient with fragile X syndrome. NSP3 binding to FMRPs disrupts their interaction with the stress granule component UBAP2L through direct competition with a peptide motif in UBAP2L to prevent FMRP incorporation into stress granules. Collectively, our results provide novel insight into how SARS-CoV-2 hijacks host cell proteins and provides molecular insight into the possible underlying molecular defects in fragile X syndrome.

Place, publisher, year, edition, pages
Springer Nature, 2024
Keywords
Fragile X Syndrome, NSP3, SARS-CoV-2, Stress Granules, UBAP2L
National Category
Infectious Medicine Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-221660 (URN)10.1038/s44319-023-00043-z (DOI)38177924 (PubMedID)2-s2.0-85185482825 (Scopus ID)
Funder
Swedish Research Council, 2018-05851
Available from: 2024-03-04 Created: 2024-03-04 Last updated: 2024-03-04Bibliographically approved
Wigren, J., Vikström, L., Rosendal, E., Gröning, R., Gwon, Y.-D., Nilsson, E., . . . Forsell, M. N. E. (2023). At-home sampling to meet geographical challenges for serological assessment of SARS-CoV-2 exposure in a rural region of northern Sweden, March to May 2021: a retrospective cohort study. Eurosurveillance, 28(13), Article ID 2200432.
Open this publication in new window or tab >>At-home sampling to meet geographical challenges for serological assessment of SARS-CoV-2 exposure in a rural region of northern Sweden, March to May 2021: a retrospective cohort study
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2023 (English)In: Eurosurveillance, ISSN 1025-496X, E-ISSN 1560-7917, Vol. 28, no 13, article id 2200432Article in journal (Refereed) Published
Abstract [en]

Background: The current SARS-CoV-2 pandemic has highlighted a need for easy and safe blood sampling in combination with accurate serological methodology. Venipuncture for testing is usually performed by trained staff at healthcare centres. Long travel distances to healthcare centres in rural regions may introduce a bias of testing towards relatively large communities with closer access. Rural regions are therefore often not represented in population-based data.

Aim: The aim of this retrospective cohort study was to develop and implement a strategy for at-home testing in a rural region of Sweden during spring 2021, and to evaluate its role to provide equal health care for its inhabitants.

Methods: We developed a sensitive method to measure antibodies to the S-protein of SARS-CoV-2 and optimised this assay for clinical use together with a strategy of at-home capillary blood sampling.

Results: We demonstrated that our ELISA gave comparable results after analysis of capillary blood or serum from SARS-CoV-2-experienced individuals. We demonstrated stability of the assay under conditions that reflected temperature and humidity during winter or summer. By assessment of capillary blood samples from 4,122 individuals, we could show both feasibility of the strategy and that implementation shifted the geographical spread of testing in favour of rural areas.

Conclusion: Implementation of at-home sampling enabled citizens living in remote rural areas access to centralised and sensitive laboratory antibody tests. The strategy for testing used here could therefore enable disease control authorities to get rapid access to information concerning immunity to infectious diseases, even across vast geographical distance.

Place, publisher, year, edition, pages
European Centre for Disease Control and Prevention (ECDC), 2023
Keywords
coronavirus disease (COVID-19), laboratory, surveillance, Sweden
National Category
Infectious Medicine Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-206673 (URN)10.2807/1560-7917.ES.2023.28.13.2200432 (DOI)000971868200003 ()36995373 (PubMedID)2-s2.0-85151573640 (Scopus ID)
Available from: 2023-04-14 Created: 2023-04-14 Last updated: 2023-09-05Bibliographically approved
Chotiwan, N., Rosendal, E., Willekens, S. M. A., Schexnaydre, E., Nilsson, E., Lindquist, R., . . . Överby, A. K. (2023). Type I interferon shapes brain distribution and tropism of tick-borne flavivirus. Nature Communications, 14(1), Article ID 2007.
Open this publication in new window or tab >>Type I interferon shapes brain distribution and tropism of tick-borne flavivirus
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2023 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 14, no 1, article id 2007Article in journal (Refereed) Published
Abstract [en]

Viral tropism within the brain and the role(s) of vertebrate immune response to neurotropic flaviviruses infection is largely understudied. We combine multimodal imaging (cm-nm scale) with single nuclei RNA-sequencing to study Langat virus in wildtype and interferon alpha/beta receptor knockout (Ifnar-/-) mice to visualize viral pathogenesis and define molecular mechanisms. Whole brain viral infection is imaged by Optical Projection Tomography coregistered to ex vivo MRI. Infection is limited to grey matter of sensory systems in wildtype mice, but extends into white matter, meninges and choroid plexus in Ifnar-/- mice. Cells in wildtype display strong type I and II IFN responses, likely due to Ifnb expressing astrocytes, infiltration of macrophages and Ifng-expressing CD8+ NK cells, whereas in Ifnar-/-, the absence of this response contributes to a shift in cellular tropism towards non-activated resident microglia. Multimodal imaging-transcriptomics exemplifies a powerful way to characterize mechanisms of viral pathogenesis and tropism.

Place, publisher, year, edition, pages
Springer Nature, 2023
National Category
Microbiology in the medical area Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Neurosciences
Identifiers
urn:nbn:se:umu:diva-206780 (URN)10.1038/s41467-023-37698-0 (DOI)000967732600009 ()37037810 (PubMedID)2-s2.0-85152115180 (Scopus ID)
Funder
The Kempe Foundations, SMK-1532Knut and Alice Wallenberg Foundation, KAW2015.0284Swedish Research Council, 2018-05851Swedish Research Council, 2017-01307Swedish Research Council, 2020-06224Swedish Research Council, 2021-06602
Available from: 2023-04-24 Created: 2023-04-24 Last updated: 2023-09-05Bibliographically approved
Kruse, T., Benz, C., Garvanska, D. H., Lindquist, R., Mihalic, F., Coscia, F., . . . Ivarsson, Y. (2021). Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities. Nature Communications, 12(1), Article ID 6761.
Open this publication in new window or tab >>Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities
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2021 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 12, no 1, article id 6761Article in journal (Refereed) Published
Abstract [en]

Viral proteins make extensive use of short peptide interaction motifs to hijack cellular host factors. However, most current large-scale methods do not identify this important class of protein-protein interactions. Uncovering peptide mediated interactions provides both a molecular understanding of viral interactions with their host and the foundation for developing novel antiviral reagents. Here we describe a viral peptide discovery approach covering 23 coronavirus strains that provides high resolution information on direct virus-host interactions. We identify 269 peptide-based interactions for 18 coronaviruses including a specific interaction between the human G3BP1/2 proteins and an ΦxFG peptide motif in the SARS-CoV-2 nucleocapsid (N) protein. This interaction supports viral replication and through its ΦxFG motif N rewires the G3BP1/2 interactome to disrupt stress granules. A peptide-based inhibitor disrupting the G3BP1/2-N interaction dampened SARS-CoV-2 infection showing that our results can be directly translated into novel specific antiviral reagents.

Place, publisher, year, edition, pages
Nature Publishing Group, 2021
National Category
Infectious Medicine
Identifiers
urn:nbn:se:umu:diva-189992 (URN)10.1038/s41467-021-26498-z (DOI)000720682600011 ()2-s2.0-85119493526 (Scopus ID)
Funder
EU, Horizon 2020Swedish Foundation for Strategic Research , SB16-0039Knut and Alice Wallenberg FoundationSwedish Research Council, 2018-03843Swedish Research Council, 2018-05851
Available from: 2021-11-30 Created: 2021-11-30 Last updated: 2023-09-05Bibliographically approved
Reimer, L., Betzer, C., Kofoed, R. H., Volbracht, C., Fog, K., Kurhade, C., . . . Jensen, P. H. (2021). PKR kinase directly regulates tau expression and Alzheimer's disease-related tau phosphorylation. Brain Pathology, 31(1), 103-119
Open this publication in new window or tab >>PKR kinase directly regulates tau expression and Alzheimer's disease-related tau phosphorylation
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2021 (English)In: Brain Pathology, ISSN 1015-6305, E-ISSN 1750-3639, Vol. 31, no 1, p. 103-119Article in journal (Refereed) Published
Abstract [en]

Deposition of extensively hyperphosphorylated tau in specific brain cells is a clear pathological hallmark in Alzheimer's disease and a number of other neurodegenerative disorders, collectively termed the tauopathies. Furthermore, hyperphosphorylation of tau prevents it from fulfilling its physiological role as a microtubule-stabilizing protein and leaves it increasingly vulnerable to self-assembly, suggestive of a central underlying role of hyperphosphorylation as a contributing factor in the etiology of these diseases. Viain vitrophosphorylation and regulation of kinase activity within cells and acute brain tissue, we reveal that the inflammation associated kinase, protein kinase R (PKR), directly phosphorylates numerous abnormal and disease-modifying residues within tau including Thr181, Ser199/202, Thr231, Ser262, Ser396, Ser404 and Ser409. Similar to disease processes, these PKR-mediated phosphorylations actively displace tau from microtubules in cells. In addition, PKR overexpression and knockdown, respectively, increase and decrease tau protein and mRNA levels in cells. This regulation occurs independent of noncoding transcriptional elements, suggesting an underlying mechanism involving intra-exonic regulation of the tau-encoding microtubule-associated protein tau (MAPT) gene. Finally, acute encephalopathy in wild type mice, induced by intracranial Langat virus infection, results in robust inflammation and PKR upregulation accompanied by abnormally phosphorylated full-length- and truncated tau. These findings indicate that PKR, independent of other kinases and upon acute brain inflammation, is capable of triggering pathological modulation of tau, which, in turn, might form the initial pathologic seed in several tauopathies such as Alzheimer's disease and Chronic traumatic encephalopathy where inflammation is severe.

Place, publisher, year, edition, pages
John Wiley & Sons, 2021
Keywords
neurodegeneration, neuroinflammation, PKR, Tau, tauopathies
National Category
Cell and Molecular Biology Neurosciences
Identifiers
urn:nbn:se:umu:diva-174348 (URN)10.1111/bpa.12883 (DOI)000556112800001 ()32716602 (PubMedID)2-s2.0-85089091967 (Scopus ID)
Available from: 2020-08-20 Created: 2020-08-20 Last updated: 2023-04-25Bibliographically approved
Gwon, Y.-D., Strand, M., Lindquist, R., Nilsson, E., Saleeb, M., Elofsson, M., . . . Evander, M. (2020). Antiviral Activity of Benzavir-2 against Emerging Flaviviruses. Viruses, 12(3), Article ID 351.
Open this publication in new window or tab >>Antiviral Activity of Benzavir-2 against Emerging Flaviviruses
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2020 (English)In: Viruses, E-ISSN 1999-4915, Vol. 12, no 3, article id 351Article in journal (Refereed) Published
Abstract [en]

Most flaviviruses are arthropod-borne viruses, transmitted by either ticks or mosquitoes, and cause morbidity and mortality worldwide. They are endemic in many countries and have recently emerged in new regions, such as the Zika virus (ZIKV) in South-and Central America, the West Nile virus (WNV) in North America, and the Yellow fever virus (YFV) in Brazil and many African countries, highlighting the need for preparedness. Currently, there are no antiviral drugs available to treat flavivirus infections. We have previously discovered a broad-spectrum antiviral compound, benzavir-2, with potent antiviral activity against both DNA- and RNA-viruses. Our purpose was to investigate the inhibitory activity of benzavir-2 against flaviviruses. We used a ZIKV ZsGreen-expressing vector, two lineages of wild-type ZIKV, and other medically important flaviviruses. Benzavir-2 inhibited ZIKV derived reporter gene expression with an EC50 value of 0.8 +/- 0.1 µM. Furthermore, ZIKV plaque formation, progeny virus production, and viral RNA expression were strongly inhibited. In addition, 2.5 µM of benzavir-2 reduced infection in vitro in three to five orders of magnitude for five other flaviviruses: WNV, YFV, the tick-borne encephalitis virus, Japanese encephalitis virus, and dengue virus. In conclusion, benzavir-2 was a potent inhibitor of flavivirus infection, which supported the broad-spectrum antiviral activity of benzavir-2.

Place, publisher, year, edition, pages
MDPI, 2020
Keywords
benzavir-2, flavivirus, Zika virus, antiviral drugs
National Category
Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-174282 (URN)10.3390/v12030351 (DOI)000525486800013 ()32235763 (PubMedID)2-s2.0-85082528703 (Scopus ID)
Funder
Swedish Research Council, 2016–06251
Available from: 2020-08-20 Created: 2020-08-20 Last updated: 2024-01-17Bibliographically approved
Uckeley, Z. M., Moeller, R., Kuhn, L. I., Nilsson, E., Robens, C., Lasswitz, L., . . . Gerold, G. (2019). Quantitative Proteomics of Uukuniemi Virus-host Cell Interactions Reveals GBF1 as Proviral Host Factor for Phleboviruses. Molecular & Cellular Proteomics, 18(12), 2401-2417
Open this publication in new window or tab >>Quantitative Proteomics of Uukuniemi Virus-host Cell Interactions Reveals GBF1 as Proviral Host Factor for Phleboviruses
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2019 (English)In: Molecular & Cellular Proteomics, ISSN 1535-9476, E-ISSN 1535-9484, Vol. 18, no 12, p. 2401-2417Article in journal (Refereed) Published
Abstract [en]

Novel tick-borne phleboviruses in the Phenuiviridae family, which are highly pathogenic in humans and all closely related to Uukuniemi virus (UUKV), have recently emerged on different continents. How phleboviruses assemble, bud, and exit cells remains largely elusive. Here, we performed high-resolution, label-free mass spectrometry analysis of UUKV immunoprecipitated from cell lysates and identified 39 cellular partners interacting with the viral envelope glycoproteins. The importance of these host factors for UUKV infection was validated by silencing each host factor by RNA interference. This revealed Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 (GBF1), a guanine nucleotide exchange factor resident in the Golgi, as a critical host factor required for the UUKV life cycle. An inhibitor of GBF1, Golgicide A, confirmed the role of the cellular factor in UUKV infection. We could pinpoint the GBF1 requirement to UUKV replication and particle assembly. When the investigation was extended to viruses from various positive and negative RNA viral families, we found that not only phleboviruses rely on GBF1 for infection, but also Flavi-, Corona-, Rhabdo-, and Togaviridae. In contrast, silencing or blocking GBF1 did not abrogate infection by the human adenovirus serotype 5 and immunodeficiency retrovirus type 1, the replication of both requires nuclear steps. Together our results indicate that UUKV relies on GBF1 for viral replication, assembly and egress. This study also highlights the proviral activity of GBF1 in the infection by a broad range of important zoonotic RNA viruses. Ticks are important vectors of infectious emerging diseases and tick-borne phleboviruses represent a growing threat to humans globally. We employed here a high-resolution, label-free mass spectrometry and RNA interference screen approach to reveal the host cell protein GBF1 as a proviral factor, not only for tick-borne phleboviruses, but also for many other important zoonotic RNA viruses. This study lays the basis for the development of innovative antiviral strategies against a broad range of human pathogenic viruses.

Place, publisher, year, edition, pages
American Society for Biochemistry and Molecular Biology, 2019
Keywords
Viruses, glycoproteins, affinity proteomics, label-free quantification, peptide mass fingerprinting, assembly, egress, GBF1, replication, Uukuniemi
National Category
Microbiology
Identifiers
urn:nbn:se:umu:diva-166821 (URN)10.1074/mcp.RA119.001631 (DOI)000501288700005 ()31570497 (PubMedID)2-s2.0-85075963172 (Scopus ID)
Funder
Knut and Alice Wallenberg FoundationSwedish Research Council, 2018-05851
Available from: 2020-01-03 Created: 2020-01-03 Last updated: 2023-11-28Bibliographically approved
Lund, H., Pieber, M., Parsa, R., Han, J., Grommisch, D., Ewing, E., . . . Harris, R. A. (2018). Competitive repopulation of an empty microglial niche yields functionally distinct subsets of microglia-like cells. Nature Communications, 9, Article ID 4845.
Open this publication in new window or tab >>Competitive repopulation of an empty microglial niche yields functionally distinct subsets of microglia-like cells
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2018 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 9, article id 4845Article in journal (Refereed) Published
Abstract [en]

Circulating monocytes can compete for virtually any tissue macrophage niche and become long-lived replacements that are phenotypically indistinguishable from their embryonic counterparts. As the factors regulating this process are incompletely understood, we studied niche competition in the brain by depleting microglia with >95% efficiency using Cx3cr1CreER/+R26DTA/+ mice and monitored long-term repopulation. Here we show that the microglial niche is repopulated within weeks by a combination of local proliferation of CX3CR1+F4/80lowClec12a microglia and infiltration of CX3CR1+F4/80hiClec12a+ macrophages that arise directly from Ly6Chi monocytes. This colonization is independent of blood brain barrier breakdown, paralleled by vascular activation, and regulated by type I interferon. Ly6Chi monocytes upregulate microglia gene expression and adopt microglia DNA methylation signatures, but retain a distinct gene signature from proliferating microglia, displaying altered surface marker expression, phagocytic capacity and cytokine production. Our results demonstrate that monocytes are imprinted by the CNS microenvironment but remain transcriptionally, epigenetically and functionally distinct.

Place, publisher, year, edition, pages
Nature Publishing Group, 2018
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-154942 (URN)10.1038/s41467-018-07295-7 (DOI)000450405300002 ()30451869 (PubMedID)2-s2.0-85056717930 (Scopus ID)
Available from: 2019-01-07 Created: 2019-01-07 Last updated: 2023-04-25Bibliographically approved
Vonderstein, K., Nilsson, E., Hubel, P., Nygård Skalman, L., Upadhyay, A., Pasto, J., . . . Överby, A. K. (2018). Viperin targets flavivirus virulence by inducing assembly of non-infectious capsid particles. Journal of Virology, 92(1), Article ID e01751-17.
Open this publication in new window or tab >>Viperin targets flavivirus virulence by inducing assembly of non-infectious capsid particles
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2018 (English)In: Journal of Virology, ISSN 0022-538X, E-ISSN 1098-5514, Vol. 92, no 1, article id e01751-17Article in journal (Refereed) Published
Abstract [en]

Efficient antiviral immunity requires interference with virus replication at multiple layers targeting diverse steps in the viral life cycle. Here we describe a novel flavivirus inhibition mechanism that results in interferon-mediated obstruction of tick-borne encephalitis virus particle assembly, and involves release of malfunctional membrane associated capsid (C) particles. This mechanism is controlled by the activity of the interferon-induced protein viperin, a broad spectrum antiviral interferon stimulated gene. Through analysis of the viperin-interactome, we identified the Golgi Brefeldin A resistant guanine nucleotide exchange factor 1 (GBF1), as the cellular protein targeted by viperin. Viperin-induced antiviral activity as well as C-particle release was stimulated by GBF1 inhibition and knock down, and reduced by elevated levels of GBF1. Our results suggest that viperin targets flavivirus virulence by inducing the secretion of unproductive non-infectious virus particles, by a GBF1-dependent mechanism. This yet undescribed antiviral mechanism allows potential therapeutic intervention.Importance The interferon response can target viral infection on almost every level, however, very little is known about interference of flavivirus assembly. Here we show that interferon, through the action of viperin, can disturb assembly of tick-borne encephalitis virus. The viperin protein is highly induced after viral infection and exhibit broad-spectrum antiviral activity. However, the mechanism of action is still elusive and appear to vary between the different viruses, indicating that cellular targets utilized by several viruses might be involved. In this study we show that viperin induce capsid particle release by interacting and inhibiting the function of the cellular protein Golgi Brefeldin A resistant guanine nucleotide exchange factor 1 (GBF1). GBF1 is a key protein in the cellular secretory pathway and essential in the life cycle of many viruses, also targeted by viperin, implicating GBF1 as a novel putative drug target.

Place, publisher, year, edition, pages
American Society of Microbiology, 2018
Keywords
COPI,  COPII,  GBF1,  assembly,  capsid,  flavivirus,  interferon,  tick-borne encephalitis virus,  viperi
National Category
Microbiology in the medical area Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-143054 (URN)10.1128/JVI.01751-17 (DOI)000417922700037 ()29046456 (PubMedID)2-s2.0-85038006738 (Scopus ID)
Funder
Swedish Research Council, 2011-2795Swedish Foundation for Strategic Research , ICA10-0059, FFL12-0089, FFL09-0181
Available from: 2017-12-14 Created: 2017-12-14 Last updated: 2023-04-24Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0001-8123-3292

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