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Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity
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Abstract
Another host factor for SARS-CoV-2: Virus-host interactions determine cellular entry and spreading in tissues. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and the earlier SARS-CoV use angiotensin-converting enzyme 2 (ACE2) as a receptor; however, their tissue tropism differs, raising the possibility that additional host factors are involved. The spike protein of SARS-CoV-2 contains a cleavage site for the protease furin that is absent from SARS-CoV (see the Perspective by Kielian). Cantuti-Castelvetri et al. now show that neuropilin-1 (NRP1), which is known to bind furin-cleaved substrates, potentiates SARS-CoV-2 infectivity. NRP1 is abundantly expressed in the respiratory and olfactory epithelium, with highest expression in endothelial and epithelial cells. Daly et al. found that the furin-cleaved S1 fragment of the spike protein binds directly to cell surface NRP1 and blocking this interaction with a small-molecule inhibitor or monoclonal antibodies reduced viral infection in cell culture. Understanding the role of NRP1 in SARS-CoV-2 infection may suggest potential targets for future antiviral therapeutics. Science , this issue p. 856 , p. 861 ; see also p. 765
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“Most recently, Neuropilin1 (NRP1) was identified as an important cofactor for entry, particularly in cells with low level ACE2 expression (Cantuti-Castelvetri et al., 2020).”
From COVID-19 and the human innate immune system (2021) · cites this paper as Cantuti-Castelvetri et al., 2020
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“Mesenchymal cells across all ages and ventricles expressed Ace2 (Angiotensin I converting enzyme 2; Figure 4J,S4J), the SARS-CoV-2 receptor, and other known and putative accessory components, including cathepsins (Ctsl and Ctsb (Muus et al., 2020)) and Neuropilin-1 (NRP1 (Cantuti-Castelvetri et al., 2020)) (Figure 4J, S4J).”
From A cellular and spatial map of the choroid plexus across brain ventricles and ages (2021) · cites this paper as Cantuti-Castelvetri et al., 2020
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“We also validated the expression of NRP1 protein, an effector of SARS-CoV-2 cell entry and infectivity, in mesenchymal cells (Cantuti-Castelvetri et al., 2020) (Figure 4M).”
From A cellular and spatial map of the choroid plexus across brain ventricles and ages (2021) · cites this paper as Cantuti-Castelvetri et al., 2020
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Gu, Y., Cao, J., Zhang, X., Gao, H., Wang, Y., Wang, J., He, J., Jiang, X., Zhang, J., Shen, G., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00595-6 · Cited by 215
Zhou, Y., Liu, Y., Gupta, S., Paramo, M. I., Hou, Y., Mao, C., Luo, Y., Judd, J., Wierbowski, S. D., Bertolotti, M., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01474-0 · Cited by 214
Leukocyte trafficking to the lungs and beyond: lessons from influenza for COVID-19
Alon, R., Sportiello, M., Kozlovski, S., Kumar, A., Reilly, E. C., Zarbock, A., Garbi, N., & Topham, D. J. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-020-00470-2 · Cited by 197
Murgolo, N., Therien, A. G., Howell, B. J., Klein, D. J., Koeplinger, K. A., Lieberman, L. A., Adam, G. C., Flynn, J. A., McKenna, P. M., Swaminathan, G., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009225 · Cited by 204
SARS-CoV-2 infection induces beta cell transdifferentiation
Tang, X., Uhl, S. A., Zhang, T., Xue, D., Li, B., Vandana, J. J., Acklin, J. A., Bonnycastle, L. L., Narisu, N., Erdos, M. R., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.05.015 · Cited by 196
Porritt, R. A., Paschold, L., Rivas, M. N., Cheng, M. H., Yonker, L. M., Chandnani, H. K., Lopez, M., Simnica, D., Schultheiß, C., Santiskulvong, C., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci146614 · Cited by 194
Laurent, Q., Martinent, R., Lim, B., Pham, A., Kato, T., López‐Andarias, J., Sakai, N., & Matile, S. (2021) · JACS Au · doi:10.1021/jacsau.1c00128 · Cited by 191
Proteolytic activation of SARS‐CoV‐2 spike protein
Takeda, M. (2021) · Microbiology and Immunology · doi:10.1111/1348-0421.12945 · Cited by 194
IL-13 is a driver of COVID-19 severity
Donlan, A. N., Sutherland, T. E., Marie, C. S., Preißner, S., Bradley, B. T., Carpenter, R. M., Sturek, J. M., Ma, J. Z., Moreau, G. B., Donowitz, J. R., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.150107 · Cited by 186
Innate immunological pathways in COVID-19 pathogenesis
Paludan, S. R., & Mogensen, T. H. (2022) · Science Immunology · doi:10.1126/sciimmunol.abm5505 · Cited by 188
Endothelium Infection and Dysregulation by SARS-CoV-2: Evidence and Caveats in COVID-19
Bernard, I., Limonta, D., Mahal, L. K., & Hobman, T. C. (2020) · Viruses · doi:10.3390/v13010029 · Cited by 187
Viral infiltration of pancreatic islets in patients with COVID-19
Steenblock, C., Richter, S., Berger, I., Barovic, M., Schmid, J., Schubert, U., Jarzebska, N., von Mäßenhausen, A., Linkermann, A., Schürmann, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23886-3 · Cited by 188
Post-viral effects of COVID-19 in the olfactory system and their implications
Xydakis, M. S., Albers, M. W., Holbrook, E. H., Lyon, D. M., Shih, R., Frasnelli, J., Pagenstecher, A., Kupke, A., Enquist, L. W., & Perlman, S. M. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(21)00182-4 · Cited by 195
The role of Neuropilin-1 in COVID-19
Mayi, B. S., Leibowitz, J. A., Woods, A. T., Ammon, K. A., Liu, A. E., & Raja, A. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009153 · Cited by 184
Hoagland, D. A., Møller, R., Uhl, S. A., Oishi, K., Frere, J. J., Golynker, I., Horiuchi, S., Panis, M., Blanco-Melo, D., Sachs, D. M., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.01.017 · Cited by 177
The Mechanism and Consequences of SARS-CoV-2 Spike-Mediated Fusion and Syncytia Formation
Rajah, M. M., Bernier, A., Buchrieser, J., & Schwartz, O. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167280 · Cited by 188
ACE2-independent infection of T lymphocytes by SARS-CoV-2
Shen, X.-R., Geng, R., Li, Q., Chen, Y., Li, S., Wang, Q. M., Min, J., Yang, Y. P., Li, B., Jiang, R.-D., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00919-x · Cited by 175
“The newly discovered binding molecules AXL and NRP1 are still dependent on ACE2 as the main receptor.(18,19) Our discovery of ACE2independent infection of T cells is surprising, but is also supported by previous discoveries that there are SARS-CoV-2 RNA cells which did not co-express ACE2 and TMPRSS2.”
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Innate metabolic responses against viral infections
Palmer, C. S. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00652-3 · Cited by 162
Acute and chronic neurological disorders in COVID-19: potential mechanisms of disease
Balcom, E. F., Nath, A., & Power, C. (2021) · Brain · doi:10.1093/brain/awab302 · Cited by 163
Zhou, Y., Xu, J., Hou, Y., Leverenz, J. B., Kallianpur, A. R., Mehra, R., Liu, Y., Yu, H., Pieper, A. A., Jehi, L. E., et al. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-021-00850-3 · Cited by 165
Peng, R., Wu, L.-A., Wang, Q., Qi, J., & Gao, G. F. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.06.001 · Cited by 168
SARS-CoV-2 spike protein co-opts VEGF-A/neuropilin-1 receptor signaling to induce analgesia
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The structural basis of accelerated host cell entry by SARS‐CoV‐2†
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What can we learn from brain autopsies in COVID-19?
Mukerji, S. S., & Solomon, I. H. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135528 · Cited by 160
TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry
Baggen, J., Jacquemyn, M., Persoons, L., Vanstreels, E., Pye, V. E., Wrobel, A. G., Calvaresi, V., Martin, S. R., Roustan, C., Cronin, N., et al. (2023) · Cell · doi:10.1016/j.cell.2023.06.005 · Cited by 159
“Recombinant ACE2 ectodomain and Wuhan-Hu-1 SARS-CoV-2 S1(1-530) were described previously.”
Mykytyn, A. Z., Breugem, T. I., Riesebosch, S., Schipper, D., van den Doel, P. B., Rottier, R. J., Lamers, M. M., & Haagmans, B. L. (2021) · eLife · doi:10.7554/elife.64508 · Cited by 153
COVID ‐19: immunopathology, pathophysiological mechanisms, and treatment options
van Eijk, L. E., Binkhorst, M., Bourgonje, A. R., Offringa, A. K., Mulder, D. J., Bos, E. M., Kolundžić, N., Abdulle, A. E., van der Voort, P. H. J., Rikkert, M. G. M. O., et al. (2021) · The Journal of Pathology · doi:10.1002/path.5642 · Cited by 156
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Human organoid models to study SARS-CoV-2 infection
Han, Y., Yang, L., Lacko, L. A., & Chen, S. (2022) · Nature Methods · doi:10.1038/s41592-022-01453-y · Cited by 158
A cohort autopsy study defines COVID-19 systemic pathogenesis
Yao, X.-H., Luo, T., Shi, Y., He, Z.-C., Tang, R., Zhang, P.-P., Cai, J., Zhou, X.-D., Jiang, D., Fei, X., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00523-8 · Cited by 148
Metadata
- Authors
- Cantuti-Castelvetri, L., Ojha, R., Pedro, L. D., Djannatian, M., Franz, J., Kuivanen, S., van der Meer, F., Kallio, K., Kaya, T., Anastasina, M., Smura, T., Levanov, L., Szirovicza, L., Tobi, A., Kallio-Kokko, H., Österlund, P., Joensuu, M., Meunier, F. A., Butcher, S. J., Winkler, M. S., Mollenhauer, B., Helenius, A., Gokce, O., Teesalu, T., Hepojoki, J., Vapalahti, O., Stadelmann, C., Balistreri, G., & Simons, M.
- Affiliations
- Institute of Neuronal Cell Biology, Technical University Munich, Munich, Germany.
- University of Helsinki (FI)
- German Center for Neurodegenerative Diseases (DE)
- Universitätsmedizin Göttingen (DE)
- Department of Neuropathology, University Medical Center Göttingen, Göttingen, Germany.
- Department of Virology, Medicum, University of Helsinki, Helsinki, Finland.
- University of Tartu (EE)
- Department of Virology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
- Finnish Institute for Health and Welfare (FI)
- The University of Queensland (AU)
- ETH Zurich (CH)
- Institute for Stroke and Dementia Research (ISD), University Hospital, LMU Munich, Munich, Germany.
- University of Zurich (CH)
- Corresponding author
- Ojha, Ravi
- Pedro, Liliana D.
- Djannatian, Minou
- Franz, Jonas
- Kuivanen, Suvi
- Balistreri, Giuseppe
- Simons, Mikael
- ORCID
- Cantuti-Castelvetri, Ludovico
- Ojha, Ravi
- Pedro, Liliana D.
- Djannatian, Minou
- Franz, Jonas
- Kuivanen, Suvi
- van der Meer, Franziska
- Kallio, Katri
- Kaya, Tuğberk
- Anastasina, Maria
- Smura, Teemu
- Levanov, Lev
- Szirovicza, Leonora
- Tobi, Allan
- Österlund, Pamela
- Joensuu, Merja
- Meunier, Frédéric A.
- Butcher, Sarah J.
- Winkler, Martin Sebastian
- Mollenhauer, Brit
- Gokce, Ozgun
- Teesalu, Tambet
- Hepojoki, Jussi
- Vapalahti, Olli
- Stadelmann, Christine
- Balistreri, Giuseppe
- Simons, Mikael
- Venue
- Science
- Published
- 2020-11-13
- Volume
- 370
- Issue
- 6518
- Pages
- 856-860
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC7857391
- OpenAlex
- W3093867667
- Cited by
- 1,925
- References
- 47
- Citations by year
- 2026: 56 · 2025: 120 · 2024: 211 · 2023: 277 · 2022: 461 · 2021: 669 · 2020: 128
- FWCI
- 50.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Science (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Open access LMU (Ludwid Maxmilian's Universitat Munchen) (submittedVersion, cc-by)
- Työväentutkimus Vuosikirja (submittedVersion)
- mediaTUM (Technical University of Munich) (submittedVersion)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, other-oa)
- Funders
- ERC CoV
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Infectious Diseases › COVID-19 Clinical Research Studies
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 detection and testing
- Keywords
- neuropilin-1, SARS-CoV-2, viral entry, furin cleavage, spike protein, host factors, viral infectivity, monoclonal antibodies, small molecule inhibitors, antiviral agents, viral tropism, ACE2
- MeSH terms
- Protein Domains, Betacoronavirus, Host Microbial Interactions, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Animals, Antibodies, Monoclonal, Female, Humans, Peptidyl-Dipeptidase A, Lung, Male, Mice, Inbred C57BL, Mutation, Olfactory Mucosa, Peptide Fragments, Pneumonia, Viral, Protein Binding, Serine Endopeptidases, Coronavirus Infections, Caco-2 Cells, Respiratory Mucosa, Neuropilin-1, Neuropilin-2, Mice, Virus Internalization, Metal Nanoparticles, HEK293 Cells, Pandemics, Spike Glycoprotein, Coronavirus
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