Crimean–Congo haemorrhagic fever virus uses LDLR to bind and enter host cells
Climate change and population densities accelerated transmission of highly pathogenic viruses to humans, including the Crimean–Congo haemorrhagic fever virus (CCHFV). Here we report that the Low Density Lipoprotein Receptor (LDLR) is a critical receptor for CCHFV cell entry, playing a vital role in...
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| Published in: | Nature microbiology Vol. 9; no. 6; pp. 1499 - 1512 |
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| Abstract | Climate change and population densities accelerated transmission of highly pathogenic viruses to humans, including the Crimean–Congo haemorrhagic fever virus (CCHFV). Here we report that the Low Density Lipoprotein Receptor (LDLR) is a critical receptor for CCHFV cell entry, playing a vital role in CCHFV infection in cell culture and blood vessel organoids. The interaction between CCHFV and LDLR is highly specific, with other members of the LDLR protein family failing to bind to or neutralize the virus. Biosensor experiments demonstrate that LDLR specifically binds the surface glycoproteins of CCHFV. Importantly, mice lacking LDLR exhibit a delay in CCHFV-induced disease. Furthermore, we identified the presence of Apolipoprotein E (ApoE) on CCHFV particles. Our findings highlight the essential role of LDLR in CCHFV infection, irrespective of ApoE presence, when the virus is produced in tick cells. This discovery holds profound implications for the development of future therapies against CCHFV.
Laboratory and clinical strains of Crimean–Congo haemorrhagic fever virus use LDLR to bind and enter host cells in blood vessel organoids and mice. Infection can also occur through ApoE, possibly present on virus particles. |
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| AbstractList | Climate change and population densities accelerated transmission of highly pathogenic viruses to humans, including the Crimean–Congo haemorrhagic fever virus (CCHFV). Here we report that the Low Density Lipoprotein Receptor (LDLR) is a critical receptor for CCHFV cell entry, playing a vital role in CCHFV infection in cell culture and blood vessel organoids. The interaction between CCHFV and LDLR is highly specific, with other members of the LDLR protein family failing to bind to or neutralize the virus. Biosensor experiments demonstrate that LDLR specifically binds the surface glycoproteins of CCHFV. Importantly, mice lacking LDLR exhibit a delay in CCHFV-induced disease. Furthermore, we identified the presence of Apolipoprotein E (ApoE) on CCHFV particles. Our findings highlight the essential role of LDLR in CCHFV infection, irrespective of ApoE presence, when the virus is produced in tick cells. This discovery holds profound implications for the development of future therapies against CCHFV.
Laboratory and clinical strains of Crimean–Congo haemorrhagic fever virus use LDLR to bind and enter host cells in blood vessel organoids and mice. Infection can also occur through ApoE, possibly present on virus particles. Climate change and population densities accelerated transmission of highly pathogenic viruses to humans, including the Crimean–Congo haemorrhagic fever virus (CCHFV). Here we report that the Low Density Lipoprotein Receptor (LDLR) is a critical receptor for CCHFV cell entry, playing a vital role in CCHFV infection in cell culture and blood vessel organoids. The interaction between CCHFV and LDLR is highly specific, with other members of the LDLR protein family failing to bind to or neutralize the virus. Biosensor experiments demonstrate that LDLR specifically binds the surface glycoproteins of CCHFV. Importantly, mice lacking LDLR exhibit a delay in CCHFV-induced disease. Furthermore, we identified the presence of Apolipoprotein E (ApoE) on CCHFV particles. Our findings highlight the essential role of LDLR in CCHFV infection, irrespective of ApoE presence, when the virus is produced in tick cells. This discovery holds profound implications for the development of future therapies against CCHFV. Climate change and population densities accelerated transmission of highly pathogenic viruses to humans, including the Crimean-Congo haemorrhagic fever virus (CCHFV). Here we report that the Low Density Lipoprotein Receptor (LDLR) is a critical receptor for CCHFV cell entry, playing a vital role in CCHFV infection in cell culture and blood vessel organoids. The interaction between CCHFV and LDLR is highly specific, with other members of the LDLR protein family failing to bind to or neutralize the virus. Biosensor experiments demonstrate that LDLR specifically binds the surface glycoproteins of CCHFV. Importantly, mice lacking LDLR exhibit a delay in CCHFV-induced disease. Furthermore, we identified the presence of Apolipoprotein E (ApoE) on CCHFV particles. Our findings highlight the essential role of LDLR in CCHFV infection, irrespective of ApoE presence, when the virus is produced in tick cells. This discovery holds profound implications for the development of future therapies against CCHFV.Climate change and population densities accelerated transmission of highly pathogenic viruses to humans, including the Crimean-Congo haemorrhagic fever virus (CCHFV). Here we report that the Low Density Lipoprotein Receptor (LDLR) is a critical receptor for CCHFV cell entry, playing a vital role in CCHFV infection in cell culture and blood vessel organoids. The interaction between CCHFV and LDLR is highly specific, with other members of the LDLR protein family failing to bind to or neutralize the virus. Biosensor experiments demonstrate that LDLR specifically binds the surface glycoproteins of CCHFV. Importantly, mice lacking LDLR exhibit a delay in CCHFV-induced disease. Furthermore, we identified the presence of Apolipoprotein E (ApoE) on CCHFV particles. Our findings highlight the essential role of LDLR in CCHFV infection, irrespective of ApoE presence, when the virus is produced in tick cells. This discovery holds profound implications for the development of future therapies against CCHFV. Climate change and population densities accelerated transmission of highly pathogenic viruses to humans, including the Crimean–Congo haemorrhagic fever virus (CCHFV). Here we report that the Low Density Lipoprotein Receptor (LDLR) is a critical receptor for CCHFV cell entry, playing a vital role in CCHFV infection in cell culture and blood vessel organoids. The interaction between CCHFV and LDLR is highly specific, with other members of the LDLR protein family failing to bind to or neutralize the virus. Biosensor experiments demonstrate that LDLR specifically binds the surface glycoproteins of CCHFV. Importantly, mice lacking LDLR exhibit a delay in CCHFV-induced disease. Furthermore, we identified the presence of Apolipoprotein E (ApoE) on CCHFV particles. Our findings highlight the essential role of LDLR in CCHFV infection, irrespective of ApoE presence, when the virus is produced in tick cells. This discovery holds profound implications for the development of future therapies against CCHFV.Laboratory and clinical strains of Crimean–Congo haemorrhagic fever virus use LDLR to bind and enter host cells in blood vessel organoids and mice. Infection can also occur through ApoE, possibly present on virus particles. |
| Author | Aastrup, Teodor Monteil, Vanessa M. Monserrat, Nuria Mirazimi, Ali Appelberg, Sofia Weber, Friedemann Kwon, Hyesoo Devignot, Stephanie Abdurahman, Samir Wright, Shane C. Dyczynski, Matheus Pittarokoilis, Ioannis Feldmann, Heinz Michlits, Georg Elder, Elizabeth Ibrahim, Ahmed Bagci, Binnur Youhanna, Sonia Kellner, Max J. Hawman, David W. Bereczky, Sándor Elaldi, Nazif Horn, Moritz Penninger, Josef M. Lauschke, Volker M. Salata, Cristiano Platzer, Sebastian W. Mirandola, Mattia |
| Author_xml | – sequence: 1 givenname: Vanessa M. orcidid: 0000-0002-2652-5695 surname: Monteil fullname: Monteil, Vanessa M. organization: Unit of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institute and Karolinska University Hospital, Public Health Agency of Sweden – sequence: 2 givenname: Shane C. orcidid: 0000-0002-7470-5068 surname: Wright fullname: Wright, Shane C. organization: Department of Physiology and Pharmacology, Karolinska Institutet – sequence: 3 givenname: Matheus surname: Dyczynski fullname: Dyczynski, Matheus organization: Acus Laboratories GmbH, JLP Health GmbH – sequence: 4 givenname: Max J. surname: Kellner fullname: Kellner, Max J. organization: IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Science, Vienna Biocenter PhD Program, a Doctoral School of the University of Vienna and the Medical University of Vienna – sequence: 5 givenname: Sofia orcidid: 0000-0002-7381-3606 surname: Appelberg fullname: Appelberg, Sofia organization: Public Health Agency of Sweden – sequence: 6 givenname: Sebastian W. orcidid: 0000-0002-2518-6273 surname: Platzer fullname: Platzer, Sebastian W. organization: IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Science, Vienna Biocenter PhD Program, a Doctoral School of the University of Vienna and the Medical University of Vienna – sequence: 7 givenname: Ahmed surname: Ibrahim fullname: Ibrahim, Ahmed organization: Attana AB – sequence: 8 givenname: Hyesoo orcidid: 0000-0003-4637-4609 surname: Kwon fullname: Kwon, Hyesoo organization: National Veterinary Institute – sequence: 9 givenname: Ioannis orcidid: 0009-0008-1510-487X surname: Pittarokoilis fullname: Pittarokoilis, Ioannis organization: Department of Physiology and Pharmacology, Karolinska Institutet – sequence: 10 givenname: Mattia surname: Mirandola fullname: Mirandola, Mattia organization: Department of Molecular Medicine, University of Padova – sequence: 11 givenname: Georg orcidid: 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Youhanna fullname: Youhanna, Sonia organization: Department of Physiology and Pharmacology, Karolinska Institutet – sequence: 18 givenname: Teodor surname: Aastrup fullname: Aastrup, Teodor organization: Attana AB – sequence: 19 givenname: Volker M. orcidid: 0000-0002-1140-6204 surname: Lauschke fullname: Lauschke, Volker M. organization: Department of Physiology and Pharmacology, Karolinska Institutet, University Tübingen, Dr. Margarete Fischer-Bosch Institute of Clinical Pharmacology – sequence: 20 givenname: Cristiano orcidid: 0000-0002-5136-7406 surname: Salata fullname: Salata, Cristiano organization: Department of Molecular Medicine, University of Padova – sequence: 21 givenname: Nazif orcidid: 0000-0002-9515-770X surname: Elaldi fullname: Elaldi, Nazif organization: Department of Infectious Diseases and Clinical Microbiology, Medical Faculty, Cumhuriyet University – sequence: 22 givenname: Friedemann orcidid: 0000-0001-9737-337X surname: Weber fullname: Weber, Friedemann organization: Institute for Virology, FB10-Veterinary Medicine, Justus-Liebig University – sequence: 23 givenname: Nuria orcidid: 0000-0002-1603-1755 surname: Monserrat fullname: Monserrat, Nuria organization: University of Barcelona, Pluripotency for Organ Regeneration, Institute for Bioengineering of Catalonia (IBEC), The Barcelona Institute of Science and Technology (BIST), Catalan Institution for Research and Advanced Studies (ICREA) – sequence: 24 givenname: David W. orcidid: 0000-0001-8233-8176 surname: Hawman fullname: Hawman, David W. organization: Rocky Mountain Laboratories, NIAID/NIH – sequence: 25 givenname: Heinz orcidid: 0000-0001-9448-8227 surname: Feldmann fullname: Feldmann, Heinz organization: Rocky Mountain Laboratories, NIAID/NIH – sequence: 26 givenname: Moritz surname: Horn fullname: Horn, Moritz organization: Acus Laboratories GmbH, JLP Health GmbH – sequence: 27 givenname: Josef M. orcidid: 0000-0002-8194-3777 surname: Penninger fullname: Penninger, Josef M. email: josef.penninger@helmholtz-hzi.de organization: IMBA, Institute of Molecular Biotechnology of the Austrian Academy of Science, Department of Laboratory Medicine, Medical University of Vienna, Helmholtz Centre for Infection Research, Department of Medical Genetics, Life Sciences Institute, University of British Columbia – sequence: 28 givenname: Ali orcidid: 0000-0003-2371-6055 surname: Mirazimi fullname: Mirazimi, Ali email: ali.mirazimi@ki.se organization: Unit of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institute and Karolinska University Hospital, Public Health Agency of Sweden, National Veterinary Institute |
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| SubjectTerms | 13/1 13/31 14/63 631/326/596/2555 631/326/596/2557 64/60 96/10 Animals Apolipoprotein E Apolipoproteins E - genetics Apolipoproteins E - metabolism Biomedical and Life Sciences Biosensors Blood vessels Cell culture Climate change Crimean hemorrhagic fever Fever Glycoproteins Hemorrhagic Fever Virus, Crimean-Congo - genetics Hemorrhagic Fever Virus, Crimean-Congo - physiology Hemorrhagic Fever, Crimean - metabolism Hemorrhagic Fever, Crimean - virology Humans Infections Infectious Diseases LDLR protein Life Sciences Low density lipoprotein Low density lipoprotein receptors Medical Microbiology Medicin och hälsovetenskap Mice Mice, Knockout Microbiology Organoids Parasitology Population density Receptor density Receptors, LDL - genetics Receptors, LDL - metabolism Receptors, Virus - metabolism Ticks - metabolism Ticks - virology Virology Virus Internalization Viruses |
| Title | Crimean–Congo haemorrhagic fever virus uses LDLR to bind and enter host cells |
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