Journal Article

DZNE-2022-00961

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity.

Cantuti-Castelvetri, L. (First author)DZNE* ; Ojha, R. ; Pedro, L. D. (First author)DZNE* ; Djannatian, M. (First author)DZNE* ; Franz, J. ; Kuivanen, S. ; van der Meer, F. ; Kallio, K. ; Kaya, T.DZNE* ; 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.Extern* ; Helenius, A. ; Gökce, O.Extern* ; Teesalu, T. ; Hepojoki, J. ; Vapalahti, O. ; Stadelmann, C.Extern* ; Balistreri, G. ; Simons, M. (Last author)DZNE*

2020
Assoc. Washington, DC

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Please use a persistent id in citations: doi:10.1126/science.abd2985

Abstract: The causative agent of coronavirus disease 2019 (COVID-19) is the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). For many viruses, tissue tropism is determined by the availability of virus receptors and entry cofactors on the surface of host cells. In this study, we found that neuropilin-1 (NRP1), known to bind furin-cleaved substrates, significantly potentiates SARS-CoV-2 infectivity, an effect blocked by a monoclonal blocking antibody against NRP1. A SARS-CoV-2 mutant with an altered furin cleavage site did not depend on NRP1 for infectivity. Pathological analysis of olfactory epithelium obtained from human COVID-19 autopsies revealed that SARS-CoV-2 infected NRP1-positive cells facing the nasal cavity. Our data provide insight into SARS-CoV-2 cell infectivity and define a potential target for antiviral intervention.

Keyword(s): Angiotensin-Converting Enzyme 2 (MeSH) ; Animals (MeSH) ; Antibodies, Monoclonal: immunology (MeSH) ; Betacoronavirus: genetics (MeSH) ; Betacoronavirus: physiology (MeSH) ; COVID-19 (MeSH) ; Caco-2 Cells (MeSH) ; Coronavirus Infections: virology (MeSH) ; Female (MeSH) ; HEK293 Cells (MeSH) ; Host Microbial Interactions (MeSH) ; Humans (MeSH) ; Lung: metabolism (MeSH) ; Male (MeSH) ; Metal Nanoparticles (MeSH) ; Mice (MeSH) ; Mice, Inbred C57BL (MeSH) ; Mutation (MeSH) ; Neuropilin-1: chemistry (MeSH) ; Neuropilin-1: genetics (MeSH) ; Neuropilin-1: immunology (MeSH) ; Neuropilin-1: metabolism (MeSH) ; Neuropilin-2: metabolism (MeSH) ; Olfactory Mucosa: metabolism (MeSH) ; Olfactory Mucosa: virology (MeSH) ; Pandemics (MeSH) ; Peptide Fragments: metabolism (MeSH) ; Peptidyl-Dipeptidase A: genetics (MeSH) ; Peptidyl-Dipeptidase A: metabolism (MeSH) ; Pneumonia, Viral: virology (MeSH) ; Protein Binding (MeSH) ; Protein Domains (MeSH) ; Respiratory Mucosa: metabolism (MeSH) ; SARS-CoV-2 (MeSH) ; Serine Endopeptidases: genetics (MeSH) ; Serine Endopeptidases: metabolism (MeSH) ; Spike Glycoprotein, Coronavirus: chemistry (MeSH) ; Spike Glycoprotein, Coronavirus: metabolism (MeSH) ; Virus Internalization (MeSH) ; Antibodies, Monoclonal ; NRP1 protein, human ; Neuropilin-2 ; Peptide Fragments ; Spike Glycoprotein, Coronavirus ; neuropilin-2, human ; spike protein, SARS-CoV-2 ; Neuropilin-1 ; Peptidyl-Dipeptidase A ; ACE2 protein, human ; Ace2 protein, mouse ; Angiotensin-Converting Enzyme 2 ; Serine Endopeptidases ; TMPRSS2 protein, human

Note: ISSN 1095-9203 not unique: **3 hits**.

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Contributing Institute(s):

1. Molecular Neurobiology (AG Simons)

Research Program(s):

1. 899 - ohne Topic (POF4-899) (POF4-899)

Appears in the scientific report 2020

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Database coverage:
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