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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
In the citing paper
“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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Mozaffari, S. A., Salehi, A., Mousavi, E., Zaman, B. A., Nassaj, A. E., Ebrahimzadeh, F., Nasiri, H., Valedkarimi, Z., Adili, A., Asemani, G., et al. (2022) · Pathology - Research and Practice · doi:10.1016/j.prp.2022.154131 · Cited by 13
“receptors and proteases, they may interact with the spike protein, revealing the multi-tissue affinity of SARS-CoV-2 (7-10).”
BackgroundYin, Y., Liu, X.-Z., Tian, Q., Fan, Y., Ye, Z., Meng, T., Wei, G., Xiong, C., Li, H., He, X., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1001558 · Cited by 13
“Identified key receptors for SARS-CoV-2 infection include ACE2 (Zhou et al., 2020), TMPRSS2 (Hoffmann et al., 2020), and NRP1 (Cantuti-Castelvetri et al., 2020) which are widely expressed in different tissues of the human body.”
BackgroundSARS‐CoV‐2 evolves to reduce but not abolish neutralizing action
Zhang, Y., Ndzouboukou, J. B., Lin, X., Hou, H., Wang, F., Yuan, L., Gan, M., Yao, Z., Fu, H., Cao, J., et al. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28207 · Cited by 12
Glycyrrhizin Inhibits SARS-CoV-2 Entry into Cells by Targeting ACE2
He, M., Liang, J.-H., Shen, Y., Zhang, J.-W., Liu, Y., Yang, K.-Y., Liu, L.-C., Wang, J., Xie, Q., Hu, C., et al. (2022) · Life · doi:10.3390/life12111706 · Cited by 13
“Among the proteins encoded by these genes, NRP1 interacts with the SARS‐CoV‐2 S1 protein, which can also facilitate SARS‐CoV‐2 cell entry and infectivity [30].”
BackgroundA snapshot of protein trafficking in SARS‐CoV‐2 infection
Prasad, V. R., & Bartenschlager, R. F. W. (2022) · Biology of the Cell · doi:10.1111/boc.202200073 · Cited by 16
“Recently, another PDZ-binding domain containing host factor, NRP1 (neuropillin-1), was identified to be important for SARS-CoV-2 entry (Cantuti-Castelvetri et al., 2020; Daly et al., 2020).”
BackgroundMolecular and cellular mechanisms involved in tissue-specific metabolic modulation by SARS-CoV-2
dos Santos, A. A. C., Rodrigues, L. E., Alecrim, A. L., Ferreira, L. D. A., Trettel, C. D. S., Gimenes, G. M., da Silva, A. F., Filho, C. P. B. S., Serdan, T. D. A., Levada‐Pires, A. C., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1037467 · Cited by 13
“The high expression of NRP1 in olfactory epithelial cells can be observed in patients with COVID-19, suggesting its role in potentiating viral infection and being the target of therapies to control the disease (Cantuti-Castelvetri et al., 2020).”
BackgroundThe Elusive Coreceptors for the SARS-CoV-2 Spike Protein
Berkowitz, R. L., & Ostrov, D. A. (2022) · Viruses · doi:10.3390/v15010067 · Cited by 16
Chee, J., Chern, B., Loh, W. S., Mullol, J., & Wang, D. Y. (2023) · Current Allergy and Asthma Reports · doi:10.1007/s11882-022-01059-6 · Cited by 13
Wang, G., Cao, J., Gui, M., Huang, P., Zhang, L. N., Qi, R., Chen, R., Lin, L., Han, Q., Lin, Y., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02848-1 · Cited by 13
“Others confirmed that NRP1 can contribute to the binding with CendR, which is found in many viruses, including EBV [49], and SARS-CoV2 [50, 51].”
BackgroundPanagiotides, N. G., Poledniczek, M., Andreas, M., Hülsmann, M., Kocher, A. A., Kopp, C. W., Piechota-Polańczyk, A., Weidenhammer, A., Pávó, N., & Wadowski, P. P. (2024) · Viruses · doi:10.3390/v16010121 · Cited by 12
Kircheis, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25105451 · Cited by 13
de Lima, M. A., Skidmore, M. A., Khanim, F. L., & Richardson, A. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.11.055 · Cited by 13
Current knowledge of COVID-19: Advances, challenges and future perspectives
Wu, Y., Peng, Z., Yan, Y., Hu, J., Wang, Y., Wang, X., Peng, R., Watterson, D., & Shi, Y. (2021) · Biosafety and Health · doi:10.1016/j.bsheal.2021.06.001 · Cited by 13
Farhangnia, P., Dehrouyeh, S., Safdarian, A. R., Farahani, S. V., Gorgani, M., Rezaei, N., Akbarpour, M., & Delbandi, A. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108786 · Cited by 14
Silva, J. R., Patricio, F., Patricio-Martínez, A., Santos‐López, G., Cedillo, L., Tizabi, Y., & Limón, I. D. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.867825 · Cited by 14
Neuropilin-1 in the pathogenesis of preeclampsia, HIV-1, and SARS-CoV-2 infection: A review
Naidoo, N., Moodley, J., Khaliq, O. P., & Naicker, T. (2022) · Virus Research · doi:10.1016/j.virusres.2022.198880 · Cited by 14
Transferrin receptor is another receptor for SARS-CoV-2 entryPreprint
Lai, R., Tang, X., Yang, M., Duan, Z., Liao, Z., Liu, L., Cheng, R., Fang, M., Gan, W., Liu, H., et al. (2020) · doi:10.21203/rs.3.rs-96962/v1 · Cited by 13
Brain mechanisms of COVID-19-sleep disordersPreprint
Semyachkina-Glushkovskaya, O. V., Тофик-Кызы, М. А., Vinnik, V., Klimova, M., Yu, T., Zhu, D., Penzel, T., & Kurths, J. (2021) · Preprints.org · doi:10.20944/preprints202105.0099.v1 · Cited by 13
SARS-CoV-2 infection activates inflammatory macrophages in vascular immune organoids
Chau, C. W., To, A., Au-Yeung, R. K. H., Tang, K., Xiang, Y., Ruan, D., Zhang, L., Wong, H., Zhang, S., Au, M. T., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-59405-9 · Cited by 12
“BSG 31 and NRP1 26,32 expressed endothelial cells, stromal cells, and monocytes.”
BackgroundInnate Receptors Expression by Lung Nociceptors: Impact on COVID-19 and Aging
Hiroki, C. H., Sarden, N., Hassanabad, M. F., & Yipp, B. G. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.785355 · Cited by 13
“Curiously, single-cell analyses have shown that olfactory sensory neurons do not express ACE2 and TMPRSS2 (100); nevertheless, Neuropilin-1, a receptor for furin-cleaved substrate, can facilitate SARS-CoV-2 infection within olfactory epithelium (101).”
BackgroundCOVID-19 and abducens nerve palsy in a 9-year-old girl—case report
Capponi, M., Cinicola, B. L., Brindisi, G., Guido, C. A., Torcé, M. C., Zicari, A. M., & Spalice, A. (2022) · The Italian Journal of Pediatrics/Italian journal of pediatrics · doi:10.1186/s13052-022-01298-3 · Cited by 12
“COVID-19: Corona Virus Disease 2019; SARS-CoV-2: Severe Acute Respiratory Syndrome Coronavirus 2; CN: Cranial Nerve; PCR: Polymerase Chain Reaction; MRI: Magnetic Resonance Imaging; CSF: Cerebro-Spinal Fluid; MFS: Miller Fisher Syndrome; GBS: Guillain-Barré Syndrome; hACE2: Human angiotensin converting enzyme 2 recept…”
BackgroundInfluentialAghamiri, S. S., Puniya, B. L., Amin, R., & Helikar, T. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1112985 · Cited by 12
“Neuropilin-1 (NRP1), the only signaling protein to be highly expressed in the third pattern, was previously shown to facilitate Sars-CoV-2 entry by interacting with spike protein (97, 98).”
BackgroundMolecular mimicry of host short linear motif-mediated interactions utilised by viruses for entry
Goswami, S., Samanta, D., & Duraivelan, K. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08389-2 · Cited by 12
Alboni, S., Secco, V., Papotti, B., Vilella, A., Adorni, M. P., Zimetti, F., Schaeffer, L., Tascedda, F., Zoli, M., Leblanc, P., et al. (2023) · Pathogens · doi:10.3390/pathogens12050647 · Cited by 12
Kal, M., Płatkowska-Adamska, B., Zarębska‐Michaluk, D., & Rzymski, P. (2023) · Journal of Personalized Medicine · doi:10.3390/jpm13060926 · Cited by 12
“Moreover, SARS-CoV-2 can alternatively utilize neuropilin 1 for cellular entry [12,13].”
BackgroundHermet, P., Delache, B., Hérate, C., Wolf, E., Kivi, G., Juronen, E., Mumm, K., Žusinaite, E., Kainov, D. E., Sankovski, E., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011532 · Cited by 13
The SARS-CoV-2 spike glycoprotein interacts with MAO-B and impairs mitochondrial energetics
Pileggi, C. A., Parmar, G., Elkhatib, H., Stewart, C. M., Alecu, I., Côté, M., Bennett, S. A. L., Sandhu, J. K., Čuperlović‐Culf, M., & Harper, M. (2023) · Current Research in Neurobiology · doi:10.1016/j.crneur.2023.100112 · Cited by 15
Scheim, D. E., Vottero, P., Santin, A. D., & Hirsh, A. G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242317039 · Cited by 18
SARS-CoV-2-Mimicking Pseudoviral Particles Accelerate α-Synuclein Aggregation In Vitro
Zilio, G., Masato, A., Sandre, M., Caregnato, A., Moret, F., Macioła, A. K., Antonini, A., Brucale, M., Cendron, L., Plotegher, N., et al. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00468 · Cited by 12
Carossino, M., Izadmehr, S., Trujillo, J. D., Gaudreault, N. N., Dittmar, W., Morozov, I., Balasuriya, U. B. R., Cordon‐Cardo, C., García‐Sastre, A., & Richt, J. A. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.03270-23 · Cited by 13
“The main determinant of susceptibility to SARS-CoV-2 is based on the binding affinity between the viral RBD of the S protein and the host ACE2 receptor, which serves as the main, but not sole, cellular receptor (56–60).”
BackgroundSARS‐CoV‐2 infection induces thymic atrophy mediated by IFN‐γ in hACE2 transgenic mice
Rizvi, Z. A., Sadhu, S., Dandotiya, J., Sharma, P., Binayke, A., Singh, V., Das, V., Khatri, R., Kumar, R., Samal, S., et al. (2024) · European Journal of Immunology · doi:10.1002/eji.202350624 · Cited by 14
“Several entry factors have been described for SARS-CoV-2 entry of which the ACE2 receptor plays a major role [30–32].”
BackgroundCell type-specific adaptation of the SARS-CoV-2 spike
Carrascosa-Sàez, M., Marqués, M.-C., IBV-Covid19-Pipeline, T., Geller, R., Elena, S. F., Rahmeh, A., Dufloo, J., & Sanjuán, R. (2024) · Virus Evolution · doi:10.1093/ve/veae032 · Cited by 13
“The major SARS-CoV-2 receptor is human ACE2 (Hoffmann et al. 2020), which is expressed in various tissues, including the gastrointestinal tract, kidney, heart, respiratory tract, and female reproductive tract (Hikmet et al. 2020).”
BackgroundVirological characteristics of a SARS-CoV-2-related bat coronavirus, BANAL-20-236
Fujita, S., Plianchaisuk, A., Deguchi, S., Ito, H., Nao, N., Wang, L., Nasser, H., Tamura, T., Kimura, I., Kashima, Y., et al. (2024) · EBioMedicine · doi:10.1016/j.ebiom.2024.105181 · Cited by 13
Bowsher, R., Marczylo, T. H., Gooch, K. E., Bailey, A., Wright, M., & Marczylo, E. L. (2024) · European Respiratory Journal · doi:10.1183/13993003.00133-2024 · Cited by 16
“Entry is further enhanced with the priming of the spike proteins of the virus by host cell enzymes transmembrane serine protease (TMPRSS) 2, furin, neuropilin (NRP)1 receptor, CD147 receptor and/or cathepsins [4 – 10].”
Flisiak, R., Jaroszewicz, J., Kozielewicz, D., Kuchar, E. P., Parczewski, M., Pawłowska, M., Piekarska, A., Rzymski, P., Simon, K. A., Tomasiewicz, K., et al. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14072305 · Cited by 13
“Alternative receptors for SARS-CoV-2 have also been detected, including ASGR1, KREMEN1, histamine receptor 1, and neuropilin 1 [15–17].”
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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