Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity-Reference-Cited by-同舟云学术

Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity

Published:2020-11-13 Issue:6518 Volume:370 Page:856-860
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Cantuti-Castelvetri Ludovico¹²^ORCID,Ojha Ravi³^ORCID,Pedro Liliana D.¹²^ORCID,Djannatian Minou¹²^ORCID,Franz Jonas⁴⁵⁶^ORCID,Kuivanen Suvi⁷^ORCID,van der Meer Franziska⁴^ORCID,Kallio Katri³,Kaya Tuğberk¹²⁸^ORCID,Anastasina Maria³⁹^ORCID,Smura Teemu⁷,Levanov Lev⁷,Szirovicza Leonora⁷^ORCID,Tobi Allan¹⁰^ORCID,Kallio-Kokko Hannimari¹¹,Österlund Pamela¹²^ORCID,Joensuu Merja¹³^ORCID,Meunier Frédéric A.¹³^ORCID,Butcher Sarah J.³⁹^ORCID,Winkler Martin Sebastian¹⁴,Mollenhauer Brit¹⁵¹⁶,Helenius Ari¹⁷,Gokce Ozgun⁸^ORCID,Teesalu Tambet³¹⁸¹⁹^ORCID,Hepojoki Jussi⁵²⁰^ORCID,Vapalahti Olli⁷¹¹²¹^ORCID,Stadelmann Christine⁴^ORCID,Balistreri Giuseppe³²²^ORCID,Simons Mikael¹²²³^ORCID

Affiliation:

1. Institute of Neuronal Cell Biology, Technical University Munich, Munich, Germany.

2. German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.

3. Faculty of Biological and Environmental Sciences, Molecular and Integrative Biosciences Research Program, University of Helsinki, Helsinki, Finland.

4. Department of Neuropathology, University Medical Center Göttingen, Göttingen, Germany.

5. Campus Institute for Dynamics of Biological Networks, University of Göttingen, Göttingen, Germany.

6. Max Planck Institute for Experimental Medicine, Göttingen, Germany.

7. Department of Virology, Medicum, University of Helsinki, Helsinki, Finland.

8. Institute for Stroke and Dementia Research (ISD), University Hospital, LMU Munich, Munich, Germany.

9. Helsinki Institute of Life Sciences–Institute of Biotechnology, University of Helsinki, Helsinki, Finland.

10. Laboratory of Cancer Biology, Institute of Biomedicine and Translational Medicine, University of Tartu, Tartu, Estonia.

11. Department of Virology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.

12. Department of Health Security, Finnish Institute for Health and Welfare (THL), Helsinki, Finland.

13. Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, Queensland, Australia.

14. Department of Anesthesiology and Intensive Care Medicine, University Medical Center Göttingen, Göttingen, Germany.

15. Department of Neurology, University Medical Center Göttingen, Göttingen, Germany.

16. Paracelsus-Elena-Klinik Kassel, Kassel, Germany.

17. Institute of Biochemistry, ETH Zürich, Zürich, Switzerland.

18. Cancer Research Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA.

19. Center for Nanomedicine and Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA, USA.

20. Institute of Veterinary Pathology, Vetsuisse Faculty, University of Zürich, Zürich, Switzerland.

21. Department of Veterinary Biosciences, University of Helsinki, Helsinki, Finland.

22. The Queensland Brain Institute, The University of Queensland, Brisbane, Queensland, Australia.

23. Munich Cluster of Systems Neurology (SyNergy), Munich, Germany.

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

Funder

ERC CoV

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference37 articles.

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