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Lindquist, Richard
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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
Öppna denna publikation i ny flik eller fönster >>The NSP3 protein of SARS-CoV-2 binds fragile X mental retardation proteins to disrupt UBAP2L interactions
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2024 (Engelska)Ingår i: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 25, nr 2, s. 902-926Artikel i tidskrift (Refereegranskat) 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.

Ort, förlag, år, upplaga, sidor
Springer Nature, 2024
Nyckelord
Fragile X Syndrome, NSP3, SARS-CoV-2, Stress Granules, UBAP2L
Nationell ämneskategori
Infektionsmedicin Biokemi och molekylärbiologi
Identifikatorer
urn:nbn:se:umu:diva-221660 (URN)10.1038/s44319-023-00043-z (DOI)38177924 (PubMedID)2-s2.0-85185482825 (Scopus ID)
Forskningsfinansiär
Vetenskapsrådet, 2018-05851
Tillgänglig från: 2024-03-04 Skapad: 2024-03-04 Senast uppdaterad: 2024-03-04Bibliografiskt granskad
Mihalič, F., Benz, C., Kassa, E., Lindquist, R., Simonetti, L., Inturi, R., . . . Ivarsson, Y. (2023). Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets. Nature Communications, 14(1), Article ID 5636.
Öppna denna publikation i ny flik eller fönster >>Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets
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2023 (Engelska)Ingår i: Nature Communications, E-ISSN 2041-1723, Vol. 14, nr 1, artikel-id 5636Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The virus life cycle depends on host-virus protein-protein interactions, which often involve a disordered protein region binding to a folded protein domain. Here, we used proteomic peptide phage display (ProP-PD) to identify peptides from the intrinsically disordered regions of the human proteome that bind to folded protein domains encoded by the SARS-CoV-2 genome. Eleven folded domains of SARS-CoV-2 proteins were found to bind 281 peptides from human proteins, and affinities of 31 interactions involving eight SARS-CoV-2 protein domains were determined (K D ∼ 7-300 μM). Key specificity residues of the peptides were established for six of the interactions. Two of the peptides, binding Nsp9 and Nsp16, respectively, inhibited viral replication. Our findings demonstrate how high-throughput peptide binding screens simultaneously identify potential host-virus interactions and peptides with antiviral properties. Furthermore, the high number of low-affinity interactions suggest that overexpression of viral proteins during infection may perturb multiple cellular pathways.

Ort, förlag, år, upplaga, sidor
Nature Publishing Group, 2023
Nationell ämneskategori
Infektionsmedicin
Identifikatorer
urn:nbn:se:umu:diva-214614 (URN)10.1038/s41467-023-41312-8 (DOI)37704626 (PubMedID)2-s2.0-85171182010 (Scopus ID)
Forskningsfinansiär
Stiftelsen för strategisk forskning (SSF), SB16-0039Vetenskapsrådet, 2020-03380Vetenskapsrådet, 2020-04395Vetenskapsrådet, 2018-05851Knut och Alice Wallenbergs Stiftelse, KAW 2020.0241Knut och Alice Wallenbergs Stiftelse, V-2020-0699
Tillgänglig från: 2023-09-27 Skapad: 2023-09-27 Senast uppdaterad: 2023-09-27Bibliografiskt granskad
Mihalič, F., Simonetti, L., Giudice, G., Sander, M. R., Lindquist, R., Peters, M. B., . . . Ivarsson, Y. (2023). Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs. Nature Communications, 14(1), Article ID 2409.
Öppna denna publikation i ny flik eller fönster >>Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs
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2023 (Engelska)Ingår i: Nature Communications, E-ISSN 2041-1723, Vol. 14, nr 1, artikel-id 2409Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Viruses mimic host short linear motifs (SLiMs) to hijack and deregulate cellular functions. Studies of motif-mediated interactions therefore provide insight into virus-host dependencies, and reveal targets for therapeutic intervention. Here, we describe the pan-viral discovery of 1712 SLiM-based virus-host interactions using a phage peptidome tiling the intrinsically disordered protein regions of 229 RNA viruses. We find mimicry of host SLiMs to be a ubiquitous viral strategy, reveal novel host proteins hijacked by viruses, and identify cellular pathways frequently deregulated by viral motif mimicry. Using structural and biophysical analyses, we show that viral mimicry-based interactions have similar binding strength and bound conformations as endogenous interactions. Finally, we establish polyadenylate-binding protein 1 as a potential target for broad-spectrum antiviral agent development. Our platform enables rapid discovery of mechanisms of viral interference and the identification of potential therapeutic targets which can aid in combating future epidemics and pandemics.

Ort, förlag, år, upplaga, sidor
Springer Nature, 2023
Nationell ämneskategori
Mikrobiologi inom det medicinska området
Identifikatorer
urn:nbn:se:umu:diva-208216 (URN)10.1038/s41467-023-38015-5 (DOI)000979744000013 ()37100772 (PubMedID)2-s2.0-85153911486 (Scopus ID)
Forskningsfinansiär
Vetenskapsrådet, 2018-05851Vetenskapsrådet, 2020-03380Vetenskapsrådet, 2020-04395Knut och Alice Wallenbergs Stiftelse, 2020.0182Stiftelsen för strategisk forskning (SSF), SB16-0039
Tillgänglig från: 2023-05-12 Skapad: 2023-05-12 Senast uppdaterad: 2023-09-05Bibliografiskt granskad
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.
Öppna denna publikation i ny flik eller fönster >>Type I interferon shapes brain distribution and tropism of tick-borne flavivirus
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2023 (Engelska)Ingår i: Nature Communications, E-ISSN 2041-1723, Vol. 14, nr 1, artikel-id 2007Artikel i tidskrift (Refereegranskat) 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.

Ort, förlag, år, upplaga, sidor
Springer Nature, 2023
Nationell ämneskategori
Mikrobiologi inom det medicinska området Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci) Neurovetenskaper
Identifikatorer
urn:nbn:se:umu:diva-206780 (URN)10.1038/s41467-023-37698-0 (DOI)000967732600009 ()37037810 (PubMedID)2-s2.0-85152115180 (Scopus ID)
Forskningsfinansiär
Kempestiftelserna, SMK-1532Knut och Alice Wallenbergs Stiftelse, KAW2015.0284Vetenskapsrådet, 2018-05851Vetenskapsrådet, 2017-01307Vetenskapsrådet, 2020-06224Vetenskapsrådet, 2021-06602
Tillgänglig från: 2023-04-24 Skapad: 2023-04-24 Senast uppdaterad: 2023-09-05Bibliografiskt granskad
Lindquist, R., Benz, C., Sereikaite, V., Maassen, L., Laursen, L., Jemth, P., . . . Överby, A. K. (2022). A syntenin inhibitor blocks endosomal entry of SARS-CoV-2 and a panel of RNA viruses. Viruses, 14(10), Article ID 2202.
Öppna denna publikation i ny flik eller fönster >>A syntenin inhibitor blocks endosomal entry of SARS-CoV-2 and a panel of RNA viruses
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2022 (Engelska)Ingår i: Viruses, E-ISSN 1999-4915, Vol. 14, nr 10, artikel-id 2202Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Viruses are dependent on host factors in order to efficiently establish an infection and replicate. Targeting the interactions of such host factors provides an attractive strategy to develop novel antivirals. Syntenin is a protein known to regulate the architecture of cellular membranes by its involvement in protein trafficking and has previously been shown to be important for human papilloma virus (HPV) infection. Here, we show that a highly potent and metabolically stable peptide inhibitor that binds to the PDZ1 domain of syntenin inhibits severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection by blocking the endosomal entry of the virus. Furthermore, we found that the inhibitor also hampered chikungunya infection and strongly reduced flavivirus infection, which is completely dependent on receptor-mediated endocytosis for their entry. In conclusion, we have identified a novel broad spectrum antiviral inhibitor that efficiently targets a broad range of RNA viruses.

Ort, förlag, år, upplaga, sidor
MDPI, 2022
Nyckelord
CHIKV, flavivirus, peptide inhibitor, SARS-CoV-2, syntenin
Nationell ämneskategori
Infektionsmedicin Mikrobiologi inom det medicinska området
Identifikatorer
urn:nbn:se:umu:diva-200890 (URN)10.3390/v14102202 (DOI)000873879700001 ()36298757 (PubMedID)2-s2.0-85140802544 (Scopus ID)
Tillgänglig från: 2022-11-09 Skapad: 2022-11-09 Senast uppdaterad: 2024-01-17Bibliografiskt granskad
Persson, B. D., Nord, S., Lindquist, R., Danskog, K., Överby, A. K., Kohl, A., . . . Arnberg, N. (2021). BAF45b is required for efficient zika virus infection of HAP1 cells. Viruses, 13(10), Article ID 2007.
Öppna denna publikation i ny flik eller fönster >>BAF45b is required for efficient zika virus infection of HAP1 cells
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2021 (Engelska)Ingår i: Viruses, E-ISSN 1999-4915, Vol. 13, nr 10, artikel-id 2007Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The 2016 Zika virus (ZIKV) epidemic illustrates the impact of flaviviruses as emerging human pathogens. For unknown reasons, ZIKV replicates more efficiently in neural progenitor cells (NPCs) than in postmitotic neurons. Here, we identified host factors used by ZIKV using the NCI-60 library of cell lines and COMPARE analysis, and cross-analyzed this library with two other libraries of host factors with importance for ZIKV infection. We identified BAF45b, a subunit of the BAF (Brg1/Brm-associated factors) protein complexes that regulate differentiation of NPCs to post-mitotic neurons. ZIKV (and other flaviviruses) infected HAP1 cells deficient in expression of BAF45b and other BAF subunits less efficiently than wildtype (WT) HAP1 cells. We concluded that subunits of the BAF complex are important for infection of ZIKV and other flavivirus. Given their function in cell and tissue differentiation, such regulators may be important determinants of tropism and pathogenesis of arthropod-borne flaviviruses.

Ort, förlag, år, upplaga, sidor
MDPI, 2021
Nyckelord
BAF45b, DPF1, Flavivirus, Zika virus
Nationell ämneskategori
Mikrobiologi inom det medicinska området Infektionsmedicin
Identifikatorer
urn:nbn:se:umu:diva-188850 (URN)10.3390/v13102007 (DOI)000792951900009 ()2-s2.0-85117010328 (Scopus ID)
Forskningsfinansiär
EU, Horisont 2020, 734584Vetenskapsrådet, 2017-02438Vetenskapsrådet, 2016-00968
Tillgänglig från: 2021-10-25 Skapad: 2021-10-25 Senast uppdaterad: 2024-01-17Bibliografiskt granskad
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.
Öppna denna publikation i ny flik eller fönster >>Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities
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2021 (Engelska)Ingår i: Nature Communications, E-ISSN 2041-1723, Vol. 12, nr 1, artikel-id 6761Artikel i tidskrift (Refereegranskat) 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.

Ort, förlag, år, upplaga, sidor
Nature Publishing Group, 2021
Nationell ämneskategori
Infektionsmedicin
Identifikatorer
urn:nbn:se:umu:diva-189992 (URN)10.1038/s41467-021-26498-z (DOI)000720682600011 ()2-s2.0-85119493526 (Scopus ID)
Forskningsfinansiär
EU, Horisont 2020Stiftelsen för strategisk forskning (SSF), SB16-0039Knut och Alice Wallenbergs StiftelseVetenskapsrådet, 2018-03843Vetenskapsrådet, 2018-05851
Tillgänglig från: 2021-11-30 Skapad: 2021-11-30 Senast uppdaterad: 2023-09-05Bibliografiskt granskad
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.
Öppna denna publikation i ny flik eller fönster >>Antiviral Activity of Benzavir-2 against Emerging Flaviviruses
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2020 (Engelska)Ingår i: Viruses, E-ISSN 1999-4915, Vol. 12, nr 3, artikel-id 351Artikel i tidskrift (Refereegranskat) 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.

Ort, förlag, år, upplaga, sidor
MDPI, 2020
Nyckelord
benzavir-2, flavivirus, Zika virus, antiviral drugs
Nationell ämneskategori
Mikrobiologi inom det medicinska området
Identifikatorer
urn:nbn:se:umu:diva-174282 (URN)10.3390/v12030351 (DOI)000525486800013 ()32235763 (PubMedID)2-s2.0-85082528703 (Scopus ID)
Forskningsfinansiär
Vetenskapsrådet, 2016–06251
Tillgänglig från: 2020-08-20 Skapad: 2020-08-20 Senast uppdaterad: 2024-01-17Bibliografiskt granskad
Wallenhammar, A., Lindquist, R., Asghar, N., Gunaltay, S., Fredlund, H., Davidsson, A., . . . Johansson, M. (2020). Revealing new tick-borne encephalitis virus foci by screening antibodies in sheep milk. Parasites & Vectors, 13(1), Article ID 185.
Öppna denna publikation i ny flik eller fönster >>Revealing new tick-borne encephalitis virus foci by screening antibodies in sheep milk
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2020 (Engelska)Ingår i: Parasites & Vectors, E-ISSN 1756-3305, Vol. 13, nr 1, artikel-id 185Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Background

Tick distribution in Sweden has increased in recent years, with the prevalence of ticks predicted to spread towards the northern parts of the country, thus increasing the risk of tick-borne zoonoses in new regions. Tick-borne encephalitis (TBE) is the most significant viral tick-borne zoonotic disease in Europe. The disease is caused by TBE virus (TBEV) infection which often leads to severe encephalitis and myelitis in humans. TBEV is usually transmitted to humans via tick bites; however, the virus can also be excreted in the milk of goats, sheep and cattle and infection may then occur via consumption of unpasteurised dairy products. Virus prevalence in questing ticks is an unreliable indicator of TBE infection risk as viral RNA is rarely detected even in large sample sizes collected at TBE-endemic areas. Hence, there is a need for robust surveillance techniques to identify emerging TBEV risk areas at early stages.

Methods

Milk and colostrum samples were collected from sheep and goats in orebro County, Sweden. The milk samples were analysed for the presence of TBEV antibodies by ELISA and validated by western blot in which milk samples were used to detect over-expressed TBEV E-protein in crude cell extracts. Neutralising titers were determined by focus reduction neutralisation test (FRNT). The stability of TBEV in milk and colostrum was studied at different temperatures.

Results

In this study we have developed a novel strategy to identify new TBEV foci. By monitoring TBEV antibodies in milk, we have identified three previously unknown foci in orebro County which also overlap with areas of TBE infection reported during 2009-2018. In addition, our data indicates that keeping unpasteurised milk at 4 degrees C will preserve the infectivity of TBEV for several days.

Conclusions

Altogether, we report a non-invasive surveillance technique for revealing risk areas for TBE in Sweden, by detecting TBEV antibodies in sheep milk. This approach is robust and reliable and can accordingly be used to map TBEV "hotspots". TBEV infectivity in refrigerated milk was preserved, emphasising the importance of pasteurisation (i.e. 72 degrees C for 15 s) prior to consumption.

Ort, förlag, år, upplaga, sidor
BMC, 2020
Nyckelord
Tick-borne encephalitis virus, Flavivirus, Tick-borne encephalitis, Hotspot, TBE virus foci, Sweden, Milk, Pasteurisation, Alimentary TBE virus transmission
Nationell ämneskategori
Infektionsmedicin
Identifikatorer
urn:nbn:se:umu:diva-171443 (URN)10.1186/s13071-020-04030-4 (DOI)000526570500001 ()32268924 (PubMedID)2-s2.0-85083113878 (Scopus ID)
Tillgänglig från: 2020-06-05 Skapad: 2020-06-05 Senast uppdaterad: 2024-01-17Bibliografiskt granskad
Lindquist, R., Rosendal, E., Weber, E., Asghar, N., Schreier, S., Lenman, A., . . . Överby, A. K. (2020). The envelope protein of tick-borne encephalitis virus influences neuron entry, pathogenicity, and vaccine protection. Journal of Neuroinflammation, 17(1), Article ID 284.
Öppna denna publikation i ny flik eller fönster >>The envelope protein of tick-borne encephalitis virus influences neuron entry, pathogenicity, and vaccine protection
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2020 (Engelska)Ingår i: Journal of Neuroinflammation, ISSN 1742-2094, E-ISSN 1742-2094, Vol. 17, nr 1, artikel-id 284Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Background: Tick-borne encephalitis virus (TBEV) is considered to be the medically most important arthropod-borne virus in Europe. The symptoms of an infection range from subclinical to mild flu-like disease to lethal encephalitis. The exact determinants of disease severity are not known; however, the virulence of the strain as well as the immune status of the host are thought to be important factors for the outcome of the infection. Here we investigated virulence determinants in TBEV infection.

Method: Mice were infected with different TBEV strains, and high virulent and low virulent TBEV strains were chosen. Sequence alignment identified differences that were cloned to generate chimera virus. The infection rate of the parental and chimeric virus were evaluated in primary mouse neurons, astrocytes, mouse embryonic fibroblasts, and in vivo. Neutralizing capacity of serum from individuals vaccinated with the FSME-IMMUN® and Encepur® or combined were evaluated.

Results: We identified a highly pathogenic and neurovirulent TBEV strain, 93/783. Using sequence analysis, we identified the envelope (E) protein of 93/783 as a potential virulence determinant and cloned it into the less pathogenic TBEV strain Torö. We found that the chimeric virus specifically infected primary neurons more efficiently compared to wild-type (WT) Torö and this correlated with enhanced pathogenicity and higher levels of viral RNA in vivo. The E protein is also the major target of neutralizing antibodies; thus, genetic variation in the E protein could influence the efficiency of the two available vaccines, FSME-IMMUN® and Encepur®. As TBEV vaccine breakthroughs have occurred in Europe, we chose to compare neutralizing capacity from individuals vaccinated with the two different vaccines or a combination of them. Our data suggest that the different vaccines do not perform equally well against the two Swedish strains.

Conclusions: Our findings show that two amino acid substitutions of the E protein found in 93/783, A83T, and A463S enhanced Torö infection of neurons as well as pathogenesis and viral replication in vivo; furthermore, we found that genetic divergence from the vaccine strain resulted in lower neutralizing antibody titers in vaccinated individuals.

Ort, förlag, år, upplaga, sidor
BioMed Central (BMC), 2020
Nationell ämneskategori
Mikrobiologi inom det medicinska området Infektionsmedicin
Identifikatorer
urn:nbn:se:umu:diva-176174 (URN)10.1186/s12974-020-01943-w (DOI)000576160400001 ()32988388 (PubMedID)2-s2.0-85092043389 (Scopus ID)
Forskningsfinansiär
Vetenskapsrådet, 2011-2795Vetenskapsrådet, 2017-02438
Tillgänglig från: 2020-10-27 Skapad: 2020-10-27 Senast uppdaterad: 2023-04-25Bibliografiskt granskad
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