Home > Publications Database > Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity. > print

001     164307
005     20240112114519.0
024 7 _ |a 10.1126/science.abd2985
|2 doi
024 7 _ |a pmid:33082293
|2 pmid
024 7 _ |a pmc:PMC7857391
|2 pmc
024 7 _ |a 0036-8075
|2 ISSN
024 7 _ |a 1095-9203
|2 ISSN
024 7 _ |a 1947-8062
|2 ISSN
024 7 _ |a altmetric:92741196
|2 altmetric
037 _ _ |a DZNE-2022-00961
041 _ _ |a English
082 _ _ |a 320
100 1 _ |a Cantuti-Castelvetri, Ludovico
|0 P:(DE-2719)2812590
|b 0
|e First author
245 _ _ |a Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity.
260 _ _ |a Washington, DC
|c 2020
|b Assoc.
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
|b journal
|m journal
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|s 1704977322_10752
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a Journal Article
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500 _ _ |a ISSN 1095-9203 not unique: **3 hits**.
520 _ _ |a 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.
536 _ _ |a 899 - ohne Topic (POF4-899)
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|f POF IV
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588 _ _ |a Dataset connected to CrossRef, PubMed, , Journals: pub.dzne.de
650 _ 7 |a Antibodies, Monoclonal
|2 NLM Chemicals
650 _ 7 |a NRP1 protein, human
|2 NLM Chemicals
650 _ 7 |a Neuropilin-2
|2 NLM Chemicals
650 _ 7 |a Peptide Fragments
|2 NLM Chemicals
650 _ 7 |a Spike Glycoprotein, Coronavirus
|2 NLM Chemicals
650 _ 7 |a neuropilin-2, human
|2 NLM Chemicals
650 _ 7 |a spike protein, SARS-CoV-2
|2 NLM Chemicals
650 _ 7 |a Neuropilin-1
|0 144713-63-3
|2 NLM Chemicals
650 _ 7 |a Peptidyl-Dipeptidase A
|0 EC 3.4.15.1
|2 NLM Chemicals
650 _ 7 |a ACE2 protein, human
|0 EC 3.4.17.23
|2 NLM Chemicals
650 _ 7 |a Ace2 protein, mouse
|0 EC 3.4.17.23
|2 NLM Chemicals
650 _ 7 |a Angiotensin-Converting Enzyme 2
|0 EC 3.4.17.23
|2 NLM Chemicals
650 _ 7 |a Serine Endopeptidases
|0 EC 3.4.21.-
|2 NLM Chemicals
650 _ 7 |a TMPRSS2 protein, human
|0 EC 3.4.21.-
|2 NLM Chemicals
650 _ 2 |a Angiotensin-Converting Enzyme 2
|2 MeSH
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Antibodies, Monoclonal: immunology
|2 MeSH
650 _ 2 |a Betacoronavirus: genetics
|2 MeSH
650 _ 2 |a Betacoronavirus: physiology
|2 MeSH
650 _ 2 |a COVID-19
|2 MeSH
650 _ 2 |a Caco-2 Cells
|2 MeSH
650 _ 2 |a Coronavirus Infections: virology
|2 MeSH
650 _ 2 |a Female
|2 MeSH
650 _ 2 |a HEK293 Cells
|2 MeSH
650 _ 2 |a Host Microbial Interactions
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Lung: metabolism
|2 MeSH
650 _ 2 |a Male
|2 MeSH
650 _ 2 |a Metal Nanoparticles
|2 MeSH
650 _ 2 |a Mice
|2 MeSH
650 _ 2 |a Mice, Inbred C57BL
|2 MeSH
650 _ 2 |a Mutation
|2 MeSH
650 _ 2 |a Neuropilin-1: chemistry
|2 MeSH
650 _ 2 |a Neuropilin-1: genetics
|2 MeSH
650 _ 2 |a Neuropilin-1: immunology
|2 MeSH
650 _ 2 |a Neuropilin-1: metabolism
|2 MeSH
650 _ 2 |a Neuropilin-2: metabolism
|2 MeSH
650 _ 2 |a Olfactory Mucosa: metabolism
|2 MeSH
650 _ 2 |a Olfactory Mucosa: virology
|2 MeSH
650 _ 2 |a Pandemics
|2 MeSH
650 _ 2 |a Peptide Fragments: metabolism
|2 MeSH
650 _ 2 |a Peptidyl-Dipeptidase A: genetics
|2 MeSH
650 _ 2 |a Peptidyl-Dipeptidase A: metabolism
|2 MeSH
650 _ 2 |a Pneumonia, Viral: virology
|2 MeSH
650 _ 2 |a Protein Binding
|2 MeSH
650 _ 2 |a Protein Domains
|2 MeSH
650 _ 2 |a Respiratory Mucosa: metabolism
|2 MeSH
650 _ 2 |a SARS-CoV-2
|2 MeSH
650 _ 2 |a Serine Endopeptidases: genetics
|2 MeSH
650 _ 2 |a Serine Endopeptidases: metabolism
|2 MeSH
650 _ 2 |a Spike Glycoprotein, Coronavirus: chemistry
|2 MeSH
650 _ 2 |a Spike Glycoprotein, Coronavirus: metabolism
|2 MeSH
650 _ 2 |a Virus Internalization
|2 MeSH
700 1 _ |a Ojha, Ravi
|0 0000-0001-7876-4607
|b 1
700 1 _ |a Pedro, Liliana Domingues
|0 P:(DE-2719)2812527
|b 2
|e First author
700 1 _ |a Djannatian, Minou
|0 P:(DE-2719)9000927
|b 3
|e First author
700 1 _ |a Franz, Jonas
|0 0000-0001-7523-6622
|b 4
700 1 _ |a Kuivanen, Suvi
|0 0000-0002-2347-5397
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700 1 _ |a van der Meer, Franziska
|0 0000-0002-9433-9173
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700 1 _ |a Kallio, Katri
|b 7
700 1 _ |a Kaya, Tugberk
|0 P:(DE-2719)9000609
|b 8
700 1 _ |a Anastasina, Maria
|0 0000-0002-4555-6446
|b 9
700 1 _ |a Smura, Teemu
|b 10
700 1 _ |a Levanov, Lev
|b 11
700 1 _ |a Szirovicza, Leonora
|0 0000-0003-1528-044X
|b 12
700 1 _ |a Tobi, Allan
|0 0000-0003-4797-5481
|b 13
700 1 _ |a Kallio-Kokko, Hannimari
|b 14
700 1 _ |a Österlund, Pamela
|0 0000-0002-2229-6661
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700 1 _ |a Joensuu, Merja
|0 0000-0002-4533-0455
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700 1 _ |a Meunier, Frédéric A
|0 0000-0001-6400-1107
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700 1 _ |a Butcher, Sarah J
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700 1 _ |a Winkler, Martin Sebastian
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700 1 _ |a Mollenhauer, Brit
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700 1 _ |a Helenius, Ari
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700 1 _ |a Gökce, Ozgun
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700 1 _ |a Teesalu, Tambet
|0 0000-0002-9458-6385
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700 1 _ |a Hepojoki, Jussi
|0 0000-0001-5699-214X
|b 24
700 1 _ |a Vapalahti, Olli
|0 0000-0003-2270-6824
|b 25
700 1 _ |a Stadelmann, Christine
|0 P:(DE-2719)9000922
|b 26
700 1 _ |a Balistreri, Giuseppe
|0 0000-0002-3585-559X
|b 27
700 1 _ |a Simons, Mikael
|0 P:(DE-2719)2811642
|b 28
|e Last author
773 _ _ |a 10.1126/science.abd2985
|g Vol. 370, no. 6518, p. 856 - 860
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|n 6518
|p 856 - 860
|t Science / Science now
|v 370
|y 2020
|x 0036-8075
856 4 _ |y OpenAccess
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