LRRC15 mediates an accessory interaction with the SARS-CoV-2 spike protein
The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component of the virus and mediates interactions essenti...
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| Published in | PLoS biology Vol. 21; no. 2; p. e3001959 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Public Library of Science
03.02.2023
Public Library of Science (PLoS) |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1545-7885 1544-9173 1545-7885 |
| DOI | 10.1371/journal.pbio.3001959 |
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| Abstract | The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component of the virus and mediates interactions essential for infection, including with the primary angiotensin-converting enzyme 2 (ACE2) receptor. We performed two independent cell-based systematic screens to determine whether there are additional proteins by which the spike protein of SARS-CoV-2 can interact with human cells. We discovered that in addition to ACE2, expression of LRRC15 also causes spike protein binding. This interaction is distinct from other known spike attachment mechanisms such as heparan sulfates or lectin receptors. Measurements of orthologous coronavirus spike proteins implied the interaction was functionally restricted to SARS-CoV-2 by accessibility. We localized the interaction to the C-terminus of the S1 domain and showed that LRRC15 shares recognition of the ACE2 receptor binding domain. From analyzing proteomics and single-cell transcriptomics, we identify LRRC15 expression as being common in human lung vasculature cells and fibroblasts. Levels of LRRC15 were greatly elevated by inflammatory signals in the lungs of COVID-19 patients. Although infection assays demonstrated that LRRC15 alone is not sufficient to permit viral entry, we present evidence that it can modulate infection of human cells. This unexpected interaction merits further investigation to determine how SARS-CoV-2 exploits host LRRC15 and whether it could account for any of the distinctive features of COVID-19. |
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| AbstractList | The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component of the virus and mediates interactions essential for infection, including with the primary angiotensin-converting enzyme 2 (ACE2) receptor. We performed two independent cell-based systematic screens to determine whether there are additional proteins by which the spike protein of SARS-CoV-2 can interact with human cells. We discovered that in addition to ACE2, expression of LRRC15 also causes spike protein binding. This interaction is distinct from other known spike attachment mechanisms such as heparan sulfates or lectin receptors. Measurements of orthologous coronavirus spike proteins implied the interaction was functionally restricted to SARS-CoV-2 by accessibility. We localized the interaction to the C-terminus of the S1 domain and showed that LRRC15 shares recognition of the ACE2 receptor binding domain. From analyzing proteomics and single-cell transcriptomics, we identify LRRC15 expression as being common in human lung vasculature cells and fibroblasts. Levels of LRRC15 were greatly elevated by inflammatory signals in the lungs of COVID-19 patients. Although infection assays demonstrated that LRRC15 alone is not sufficient to permit viral entry, we present evidence that it can modulate infection of human cells. This unexpected interaction merits further investigation to determine how SARS-CoV-2 exploits host LRRC15 and whether it could account for any of the distinctive features of COVID-19. The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component of the virus and mediates interactions essential for infection, including with the primary angiotensin-converting enzyme 2 (ACE2) receptor. We performed two independent cell-based systematic screens to determine whether there are additional proteins by which the spike protein of SARS-CoV-2 can interact with human cells. We discovered that in addition to ACE2, expression of LRRC15 also causes spike protein binding. This interaction is distinct from other known spike attachment mechanisms such as heparan sulfates or lectin receptors. Measurements of orthologous coronavirus spike proteins implied the interaction was functionally restricted to SARS-CoV-2 by accessibility. We localized the interaction to the C-terminus of the S1 domain and showed that LRRC15 shares recognition of the ACE2 receptor binding domain. From analyzing proteomics and single-cell transcriptomics, we identify LRRC15 expression as being common in human lung vasculature cells and fibroblasts. Levels of LRRC15 were greatly elevated by inflammatory signals in the lungs of COVID-19 patients. Although infection assays demonstrated that LRRC15 alone is not sufficient to permit viral entry, we present evidence that it can modulate infection of human cells. This unexpected interaction merits further investigation to determine how SARS-CoV-2 exploits host LRRC15 and whether it could account for any of the distinctive features of COVID-19. A systematic search for human proteins that can bind to the spike protein of SARS-CoV-2 reveals that LRRC15 can act as a host factor for the virus, and may therefore modulate infection with potential implications for COVID-19. The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component of the virus and mediates interactions essential for infection, including with the primary angiotensin-converting enzyme 2 (ACE2) receptor. We performed two independent cell-based systematic screens to determine whether there are additional proteins by which the spike protein of SARS-CoV-2 can interact with human cells. We discovered that in addition to ACE2, expression of LRRC15 also causes spike protein binding. This interaction is distinct from other known spike attachment mechanisms such as heparan sulfates or lectin receptors. Measurements of orthologous coronavirus spike proteins implied the interaction was functionally restricted to SARS-CoV-2 by accessibility. We localized the interaction to the C-terminus of the S1 domain and showed that LRRC15 shares recognition of the ACE2 receptor binding domain. From analyzing proteomics and single-cell transcriptomics, we identify LRRC15 expression as being common in human lung vasculature cells and fibroblasts. Levels of LRRC15 were greatly elevated by inflammatory signals in the lungs of COVID-19 patients. Although infection assays demonstrated that LRRC15 alone is not sufficient to permit viral entry, we present evidence that it can modulate infection of human cells. This unexpected interaction merits further investigation to determine how SARS-CoV-2 exploits host LRRC15 and whether it could account for any of the distinctive features of COVID-19.The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component of the virus and mediates interactions essential for infection, including with the primary angiotensin-converting enzyme 2 (ACE2) receptor. We performed two independent cell-based systematic screens to determine whether there are additional proteins by which the spike protein of SARS-CoV-2 can interact with human cells. We discovered that in addition to ACE2, expression of LRRC15 also causes spike protein binding. This interaction is distinct from other known spike attachment mechanisms such as heparan sulfates or lectin receptors. Measurements of orthologous coronavirus spike proteins implied the interaction was functionally restricted to SARS-CoV-2 by accessibility. We localized the interaction to the C-terminus of the S1 domain and showed that LRRC15 shares recognition of the ACE2 receptor binding domain. From analyzing proteomics and single-cell transcriptomics, we identify LRRC15 expression as being common in human lung vasculature cells and fibroblasts. Levels of LRRC15 were greatly elevated by inflammatory signals in the lungs of COVID-19 patients. Although infection assays demonstrated that LRRC15 alone is not sufficient to permit viral entry, we present evidence that it can modulate infection of human cells. This unexpected interaction merits further investigation to determine how SARS-CoV-2 exploits host LRRC15 and whether it could account for any of the distinctive features of COVID-19. The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component of the virus and mediates interactions essential for infection, including with the primary angiotensin-converting enzyme 2 (ACE2) receptor. We performed two independent cell-based systematic screens to determine whether there are additional proteins by which the spike protein of SARS-CoV-2 can interact with human cells. We discovered that in addition to ACE2, expression of LRRC15 also causes spike protein binding. This interaction is distinct from other known spike attachment mechanisms such as heparan sulfates or lectin receptors. Measurements of orthologous coronavirus spike proteins implied the interaction was functionally restricted to SARS-CoV-2 by accessibility. We localized the interaction to the C-terminus of the S1 domain and showed that LRRC15 shares recognition of the ACE2 receptor binding domain. From analyzing proteomics and single-cell transcriptomics, we identify LRRC15 expression as being common in human lung vasculature cells and fibroblasts. Levels of LRRC15 were greatly elevated by inflammatory signals in the lungs of COVID-19 patients. Although infection assays demonstrated that LRRC15 alone is not sufficient to permit viral entry, we present evidence that it can modulate infection of human cells. This unexpected interaction merits further investigation to determine how SARS-CoV-2 exploits host LRRC15 and whether it could account for any of the distinctive features of COVID-19. A systematic search for human proteins that can bind to the spike protein of SARS-CoV-2 reveals that LRRC15 can act as a host factor for the virus, and may therefore modulate infection with potential implications for COVID-19. |
| Audience | Academic |
| Author | Watson, Samuel James Gabaev, Ildar Greenwood, Edward J. D. Gawden-Bone, Christian M. Ortmann, Brian M. Matheson, Nicholas J. Crozier, Thomas W. M. Wright, Gavin J. Hoffmann, Markus Teixeira-Silva, Ana Pauzaite, Tekle Gerber, Pehuén Pereyra Shilts, Jarrod Nathan, James A. Lehner, Paul J. Pöhlmann, Stefan |
| AuthorAffiliation | 1 Cell Surface Signalling Laboratory, Wellcome Sanger Institute, Cambridge, United Kingdom 6 NHS Blood and Transplant, Cambridge, United Kingdom New York University School of Medicine, UNITED STATES 2 Department of Biology, Hull York Medical School, York Biomedical Research Institute, University of York, York, United Kingdom 3 Department of Medicine, Cambridge Institute of Therapeutic Immunology and Infectious Disease, University of Cambridge, Cambridge, United Kingdom 5 Faculty of Biology and Psychology, Georg-August University Göttingen, Göttingen, Germany 4 Infection Biology Unit, German Primate Center – Leibniz Institute for Primate Research, Göttingen, Germany |
| AuthorAffiliation_xml | – name: 5 Faculty of Biology and Psychology, Georg-August University Göttingen, Göttingen, Germany – name: New York University School of Medicine, UNITED STATES – name: 6 NHS Blood and Transplant, Cambridge, United Kingdom – name: 3 Department of Medicine, Cambridge Institute of Therapeutic Immunology and Infectious Disease, University of Cambridge, Cambridge, United Kingdom – name: 4 Infection Biology Unit, German Primate Center – Leibniz Institute for Primate Research, Göttingen, Germany – name: 1 Cell Surface Signalling Laboratory, Wellcome Sanger Institute, Cambridge, United Kingdom – name: 2 Department of Biology, Hull York Medical School, York Biomedical Research Institute, University of York, York, United Kingdom |
| Author_xml | – sequence: 1 givenname: Jarrod orcidid: 0000-0002-0959-0583 surname: Shilts fullname: Shilts, Jarrod – sequence: 2 givenname: Thomas W. M. orcidid: 0000-0003-0951-4588 surname: Crozier fullname: Crozier, Thomas W. M. – sequence: 3 givenname: Ana orcidid: 0000-0002-9011-9501 surname: Teixeira-Silva fullname: Teixeira-Silva, Ana – sequence: 4 givenname: Ildar surname: Gabaev fullname: Gabaev, Ildar – sequence: 5 givenname: Pehuén Pereyra surname: Gerber fullname: Gerber, Pehuén Pereyra – sequence: 6 givenname: Edward J. D. orcidid: 0000-0002-5224-0263 surname: Greenwood fullname: Greenwood, Edward J. D. – sequence: 7 givenname: Samuel James surname: Watson fullname: Watson, Samuel James – sequence: 8 givenname: Brian M. surname: Ortmann fullname: Ortmann, Brian M. – sequence: 9 givenname: Christian M. orcidid: 0000-0003-0413-3727 surname: Gawden-Bone fullname: Gawden-Bone, Christian M. – sequence: 10 givenname: Tekle orcidid: 0000-0002-0668-3661 surname: Pauzaite fullname: Pauzaite, Tekle – sequence: 11 givenname: Markus orcidid: 0000-0003-4603-7696 surname: Hoffmann fullname: Hoffmann, Markus – sequence: 12 givenname: James A. orcidid: 0000-0002-0248-1632 surname: Nathan fullname: Nathan, James A. – sequence: 13 givenname: Stefan orcidid: 0000-0001-6086-9136 surname: Pöhlmann fullname: Pöhlmann, Stefan – sequence: 14 givenname: Nicholas J. surname: Matheson fullname: Matheson, Nicholas J. – sequence: 15 givenname: Paul J. orcidid: 0000-0001-9383-1054 surname: Lehner fullname: Lehner, Paul J. – sequence: 16 givenname: Gavin J. orcidid: 0000-0003-0537-0863 surname: Wright fullname: Wright, Gavin J. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/36735681$$D View this record in MEDLINE/PubMed |
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| Copyright | Copyright: © 2023 Shilts et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. COPYRIGHT 2023 Public Library of Science 2023 Shilts et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2023 Shilts et al 2023 Shilts et al |
| Copyright_xml | – notice: Copyright: © 2023 Shilts et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. – notice: COPYRIGHT 2023 Public Library of Science – notice: 2023 Shilts et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: 2023 Shilts et al 2023 Shilts et al |
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| SubjectTerms | ACE2 Analysis Angiotensin Angiotensin-converting enzyme 2 Angiotensin-Converting Enzyme 2 - metabolism Binding Binding proteins Biology and life sciences C-Terminus Cells Cloning Coronaviruses COVID-19 CRISPR Domains Enzymes Fibroblasts Flow cytometry Gene expression Genes Genomes Heparan sulfate Humans Identification and classification Inflammation Lungs Medicine and health sciences Membrane Proteins - metabolism Peptidyl-dipeptidase A Properties Protein Binding Proteins Proteomics Receptors Research and Analysis Methods Respiratory diseases SARS-CoV-2 - metabolism Severe acute respiratory syndrome coronavirus 2 Short Reports Spike Glycoprotein, Coronavirus - metabolism Spike protein Transcription factors Transcriptomics Viral diseases Viral infections Viruses |
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| Title | LRRC15 mediates an accessory interaction with the SARS-CoV-2 spike protein |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/36735681 https://www.proquest.com/docview/2787641555 https://www.proquest.com/docview/2773116610 https://pubmed.ncbi.nlm.nih.gov/PMC9897555 https://doaj.org/article/90f98ee96aff4b489c474fa416cf8b43 |
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