TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry
SARS-CoV-2 is associated with broad tissue tropism, a characteristic often determined by the availability of entry receptors on host cells. Here, we show that TMEM106B, a lysosomal transmembrane protein, can serve as an alternative receptor for SARS-CoV-2 entry into angiotensin-converting enzyme 2 (...
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| Veröffentlicht in: | Cell Jg. 186; H. 16; S. 3427 |
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03.08.2023
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| Abstract | SARS-CoV-2 is associated with broad tissue tropism, a characteristic often determined by the availability of entry receptors on host cells. Here, we show that TMEM106B, a lysosomal transmembrane protein, can serve as an alternative receptor for SARS-CoV-2 entry into angiotensin-converting enzyme 2 (ACE2)-negative cells. Spike substitution E484D increased TMEM106B binding, thereby enhancing TMEM106B-mediated entry. TMEM106B-specific monoclonal antibodies blocked SARS-CoV-2 infection, demonstrating a role of TMEM106B in viral entry. Using X-ray crystallography, cryogenic electron microscopy (cryo-EM), and hydrogen-deuterium exchange mass spectrometry (HDX-MS), we show that the luminal domain (LD) of TMEM106B engages the receptor-binding motif of SARS-CoV-2 spike. Finally, we show that TMEM106B promotes spike-mediated syncytium formation, suggesting a role of TMEM106B in viral fusion. Together, our findings identify an ACE2-independent SARS-CoV-2 infection mechanism that involves cooperative interactions with the receptors heparan sulfate and TMEM106B. |
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| AbstractList | SARS-CoV-2 is associated with broad tissue tropism, a characteristic often determined by the availability of entry receptors on host cells. Here, we show that TMEM106B, a lysosomal transmembrane protein, can serve as an alternative receptor for SARS-CoV-2 entry into angiotensin-converting enzyme 2 (ACE2)-negative cells. Spike substitution E484D increased TMEM106B binding, thereby enhancing TMEM106B-mediated entry. TMEM106B-specific monoclonal antibodies blocked SARS-CoV-2 infection, demonstrating a role of TMEM106B in viral entry. Using X-ray crystallography, cryogenic electron microscopy (cryo-EM), and hydrogen-deuterium exchange mass spectrometry (HDX-MS), we show that the luminal domain (LD) of TMEM106B engages the receptor-binding motif of SARS-CoV-2 spike. Finally, we show that TMEM106B promotes spike-mediated syncytium formation, suggesting a role of TMEM106B in viral fusion. Together, our findings identify an ACE2-independent SARS-CoV-2 infection mechanism that involves cooperative interactions with the receptors heparan sulfate and TMEM106B.SARS-CoV-2 is associated with broad tissue tropism, a characteristic often determined by the availability of entry receptors on host cells. Here, we show that TMEM106B, a lysosomal transmembrane protein, can serve as an alternative receptor for SARS-CoV-2 entry into angiotensin-converting enzyme 2 (ACE2)-negative cells. Spike substitution E484D increased TMEM106B binding, thereby enhancing TMEM106B-mediated entry. TMEM106B-specific monoclonal antibodies blocked SARS-CoV-2 infection, demonstrating a role of TMEM106B in viral entry. Using X-ray crystallography, cryogenic electron microscopy (cryo-EM), and hydrogen-deuterium exchange mass spectrometry (HDX-MS), we show that the luminal domain (LD) of TMEM106B engages the receptor-binding motif of SARS-CoV-2 spike. Finally, we show that TMEM106B promotes spike-mediated syncytium formation, suggesting a role of TMEM106B in viral fusion. Together, our findings identify an ACE2-independent SARS-CoV-2 infection mechanism that involves cooperative interactions with the receptors heparan sulfate and TMEM106B. SARS-CoV-2 is associated with broad tissue tropism, a characteristic often determined by the availability of entry receptors on host cells. Here, we show that TMEM106B, a lysosomal transmembrane protein, can serve as an alternative receptor for SARS-CoV-2 entry into angiotensin-converting enzyme 2 (ACE2)-negative cells. Spike substitution E484D increased TMEM106B binding, thereby enhancing TMEM106B-mediated entry. TMEM106B-specific monoclonal antibodies blocked SARS-CoV-2 infection, demonstrating a role of TMEM106B in viral entry. Using X-ray crystallography, cryogenic electron microscopy (cryo-EM), and hydrogen-deuterium exchange mass spectrometry (HDX-MS), we show that the luminal domain (LD) of TMEM106B engages the receptor-binding motif of SARS-CoV-2 spike. Finally, we show that TMEM106B promotes spike-mediated syncytium formation, suggesting a role of TMEM106B in viral fusion. Together, our findings identify an ACE2-independent SARS-CoV-2 infection mechanism that involves cooperative interactions with the receptors heparan sulfate and TMEM106B. |
| Author | Cherepanov, Peter Calvaresi, Valeria Reading, Eamonn De Smet, Frederik Daelemans, Dirk Pye, Valerie E Rhinn, Herve Maes, Piet Brown, Eric Yee, Angie Vanstreels, Els Martin, Stephen R Ah Young-Chapon, Maxime Baggen, Jim Cronin, Nora B Roustan, Chloë Wrobel, Antoni G Jacquemyn, Maarten Vercruysse, Thomas Mamchak, Alusha Andre Persoons, Leentje Nivitchanyong, Toey Franco-Hernandez, Natalia Thibaut, Hendrik Jan Roell, Marina |
| Author_xml | – sequence: 1 givenname: Jim surname: Baggen fullname: Baggen, Jim email: jim.baggen@kuleuven.be organization: KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven 3000, Belgium. Electronic address: jim.baggen@kuleuven.be – sequence: 2 givenname: Maarten surname: Jacquemyn fullname: Jacquemyn, Maarten organization: KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven 3000, Belgium – sequence: 3 givenname: Leentje surname: Persoons fullname: Persoons, Leentje organization: KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven 3000, Belgium – sequence: 4 givenname: Els surname: Vanstreels fullname: Vanstreels, Els organization: KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven 3000, Belgium – sequence: 5 givenname: Valerie E surname: Pye fullname: Pye, Valerie E organization: Chromatin Structure and Mobile DNA Laboratory, Francis Crick Institute, London NW1 1AT, UK – sequence: 6 givenname: Antoni G surname: Wrobel fullname: Wrobel, Antoni G organization: Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London NW1 1AT, UK – sequence: 7 givenname: Valeria surname: Calvaresi fullname: Calvaresi, Valeria organization: Department of Chemistry, Britannia House, 7 Trinity Street, King's College London, London SE1 1DB, UK – sequence: 8 givenname: Stephen R surname: Martin fullname: Martin, Stephen R organization: Structural Biology of Disease Processes Laboratory, Francis Crick Institute, London NW1 1AT, UK – sequence: 9 givenname: Chloë surname: Roustan fullname: Roustan, Chloë organization: Structural Biology Science Technology Platform, Francis Crick Institute, London NW1 1AT, UK – sequence: 10 givenname: Nora B surname: Cronin fullname: Cronin, Nora B organization: LonCEM Facility, Francis Crick Institute, London NW1 1AT, UK – sequence: 11 givenname: Eamonn surname: Reading fullname: Reading, Eamonn organization: Department of Chemistry, Britannia House, 7 Trinity Street, King's College London, London SE1 1DB, UK – sequence: 12 givenname: Hendrik Jan surname: Thibaut fullname: Thibaut, Hendrik Jan organization: KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Translational Platform Virology and Chemotherapy, Rega Institute, Leuven 3000, Belgium – sequence: 13 givenname: Thomas surname: Vercruysse fullname: Vercruysse, Thomas organization: KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Translational Platform Virology and Chemotherapy, Rega Institute, Leuven 3000, Belgium – sequence: 14 givenname: Piet surname: Maes fullname: Maes, Piet organization: KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Clinical and Epidemiological Virology, Rega Institute, Leuven 3000, Belgium – sequence: 15 givenname: Frederik surname: De Smet fullname: De Smet, Frederik organization: KU Leuven Department of Imaging and Pathology, Laboratory for Precision Cancer Medicine, Translational Cell and Tissue Research Unit, Leuven 3000, Belgium – sequence: 16 givenname: Angie surname: Yee fullname: Yee, Angie organization: Alector LLC, 131 Oyster Point Blvd. Suite 600, South San Francisco, CA 94080, USA – sequence: 17 givenname: Toey surname: Nivitchanyong fullname: Nivitchanyong, Toey organization: Alector LLC, 131 Oyster Point Blvd. Suite 600, South San Francisco, CA 94080, USA – sequence: 18 givenname: Marina surname: Roell fullname: Roell, Marina organization: Alector LLC, 131 Oyster Point Blvd. Suite 600, South San Francisco, CA 94080, USA – sequence: 19 givenname: Natalia surname: Franco-Hernandez fullname: Franco-Hernandez, Natalia organization: Alector LLC, 131 Oyster Point Blvd. Suite 600, South San Francisco, CA 94080, USA – sequence: 20 givenname: Herve surname: Rhinn fullname: Rhinn, Herve organization: Alector LLC, 131 Oyster Point Blvd. Suite 600, South San Francisco, CA 94080, USA – sequence: 21 givenname: Alusha Andre surname: Mamchak fullname: Mamchak, Alusha Andre organization: Alector LLC, 131 Oyster Point Blvd. Suite 600, South San Francisco, CA 94080, USA – sequence: 22 givenname: Maxime surname: Ah Young-Chapon fullname: Ah Young-Chapon, Maxime organization: Alector LLC, 131 Oyster Point Blvd. Suite 600, South San Francisco, CA 94080, USA – sequence: 23 givenname: Eric surname: Brown fullname: Brown, Eric organization: Alector LLC, 131 Oyster Point Blvd. Suite 600, South San Francisco, CA 94080, USA – sequence: 24 givenname: Peter surname: Cherepanov fullname: Cherepanov, Peter email: peter.cherepanov@crick.ac.uk organization: Chromatin Structure and Mobile DNA Laboratory, Francis Crick Institute, London NW1 1AT, UK; Department of Infectious Disease, Section of Virology, Imperial College London, St Mary's Campus, Norfolk Place, London W2 1PG, UK. Electronic address: peter.cherepanov@crick.ac.uk – sequence: 25 givenname: Dirk surname: Daelemans fullname: Daelemans, Dirk email: dirk.daelemans@kuleuven.be organization: KU Leuven Department of Microbiology, Immunology and Transplantation, Laboratory of Virology and Chemotherapy, Rega Institute, Leuven 3000, Belgium. Electronic address: dirk.daelemans@kuleuven.be |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/37421949$$D View this record in MEDLINE/PubMed |
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| Keywords | SARS-CoV-2 TMEM106B crystal structure ACE2-independent entry antibody neutralization TMEM106B coronavirus cryo-EM entry receptor |
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| Title | TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry |
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