000164307 001__ 164307
000164307 005__ 20240112114519.0
000164307 0247_ $$2doi$$a10.1126/science.abd2985
000164307 0247_ $$2pmid$$apmid:33082293
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000164307 0247_ $$2ISSN$$a0036-8075
000164307 0247_ $$2ISSN$$a1095-9203
000164307 0247_ $$2ISSN$$a1947-8062
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000164307 037__ $$aDZNE-2022-00961
000164307 041__ $$aEnglish
000164307 082__ $$a320
000164307 1001_ $$0P:(DE-2719)2812590$$aCantuti-Castelvetri, Ludovico$$b0$$eFirst author
000164307 245__ $$aNeuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity.
000164307 260__ $$aWashington, DC$$bAssoc.$$c2020
000164307 3367_ $$2DRIVER$$aarticle
000164307 3367_ $$2DataCite$$aOutput Types/Journal article
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000164307 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000164307 3367_ $$00$$2EndNote$$aJournal Article
000164307 500__ $$aISSN 1095-9203 not unique: **3 hits**.
000164307 520__ $$aThe 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.
000164307 536__ $$0G:(DE-HGF)POF4-899$$a899 - ohne Topic (POF4-899)$$cPOF4-899$$fPOF IV$$x0
000164307 588__ $$aDataset connected to CrossRef, PubMed, , Journals: pub.dzne.de
000164307 650_7 $$2NLM Chemicals$$aAntibodies, Monoclonal
000164307 650_7 $$2NLM Chemicals$$aNRP1 protein, human
000164307 650_7 $$2NLM Chemicals$$aNeuropilin-2
000164307 650_7 $$2NLM Chemicals$$aPeptide Fragments
000164307 650_7 $$2NLM Chemicals$$aSpike Glycoprotein, Coronavirus
000164307 650_7 $$2NLM Chemicals$$aneuropilin-2, human
000164307 650_7 $$2NLM Chemicals$$aspike protein, SARS-CoV-2
000164307 650_7 $$0144713-63-3$$2NLM Chemicals$$aNeuropilin-1
000164307 650_7 $$0EC 3.4.15.1$$2NLM Chemicals$$aPeptidyl-Dipeptidase A
000164307 650_7 $$0EC 3.4.17.23$$2NLM Chemicals$$aACE2 protein, human
000164307 650_7 $$0EC 3.4.17.23$$2NLM Chemicals$$aAce2 protein, mouse
000164307 650_7 $$0EC 3.4.17.23$$2NLM Chemicals$$aAngiotensin-Converting Enzyme 2
000164307 650_7 $$0EC 3.4.21.-$$2NLM Chemicals$$aSerine Endopeptidases
000164307 650_7 $$0EC 3.4.21.-$$2NLM Chemicals$$aTMPRSS2 protein, human
000164307 650_2 $$2MeSH$$aAngiotensin-Converting Enzyme 2
000164307 650_2 $$2MeSH$$aAnimals
000164307 650_2 $$2MeSH$$aAntibodies, Monoclonal: immunology
000164307 650_2 $$2MeSH$$aBetacoronavirus: genetics
000164307 650_2 $$2MeSH$$aBetacoronavirus: physiology
000164307 650_2 $$2MeSH$$aCOVID-19
000164307 650_2 $$2MeSH$$aCaco-2 Cells
000164307 650_2 $$2MeSH$$aCoronavirus Infections: virology
000164307 650_2 $$2MeSH$$aFemale
000164307 650_2 $$2MeSH$$aHEK293 Cells
000164307 650_2 $$2MeSH$$aHost Microbial Interactions
000164307 650_2 $$2MeSH$$aHumans
000164307 650_2 $$2MeSH$$aLung: metabolism
000164307 650_2 $$2MeSH$$aMale
000164307 650_2 $$2MeSH$$aMetal Nanoparticles
000164307 650_2 $$2MeSH$$aMice
000164307 650_2 $$2MeSH$$aMice, Inbred C57BL
000164307 650_2 $$2MeSH$$aMutation
000164307 650_2 $$2MeSH$$aNeuropilin-1: chemistry
000164307 650_2 $$2MeSH$$aNeuropilin-1: genetics
000164307 650_2 $$2MeSH$$aNeuropilin-1: immunology
000164307 650_2 $$2MeSH$$aNeuropilin-1: metabolism
000164307 650_2 $$2MeSH$$aNeuropilin-2: metabolism
000164307 650_2 $$2MeSH$$aOlfactory Mucosa: metabolism
000164307 650_2 $$2MeSH$$aOlfactory Mucosa: virology
000164307 650_2 $$2MeSH$$aPandemics
000164307 650_2 $$2MeSH$$aPeptide Fragments: metabolism
000164307 650_2 $$2MeSH$$aPeptidyl-Dipeptidase A: genetics
000164307 650_2 $$2MeSH$$aPeptidyl-Dipeptidase A: metabolism
000164307 650_2 $$2MeSH$$aPneumonia, Viral: virology
000164307 650_2 $$2MeSH$$aProtein Binding
000164307 650_2 $$2MeSH$$aProtein Domains
000164307 650_2 $$2MeSH$$aRespiratory Mucosa: metabolism
000164307 650_2 $$2MeSH$$aSARS-CoV-2
000164307 650_2 $$2MeSH$$aSerine Endopeptidases: genetics
000164307 650_2 $$2MeSH$$aSerine Endopeptidases: metabolism
000164307 650_2 $$2MeSH$$aSpike Glycoprotein, Coronavirus: chemistry
000164307 650_2 $$2MeSH$$aSpike Glycoprotein, Coronavirus: metabolism
000164307 650_2 $$2MeSH$$aVirus Internalization
000164307 7001_ $$00000-0001-7876-4607$$aOjha, Ravi$$b1
000164307 7001_ $$0P:(DE-2719)2812527$$aPedro, Liliana Domingues$$b2$$eFirst author
000164307 7001_ $$0P:(DE-2719)9000927$$aDjannatian, Minou$$b3$$eFirst author
000164307 7001_ $$00000-0001-7523-6622$$aFranz, Jonas$$b4
000164307 7001_ $$00000-0002-2347-5397$$aKuivanen, Suvi$$b5
000164307 7001_ $$00000-0002-9433-9173$$avan der Meer, Franziska$$b6
000164307 7001_ $$aKallio, Katri$$b7
000164307 7001_ $$0P:(DE-2719)9000609$$aKaya, Tugberk$$b8
000164307 7001_ $$00000-0002-4555-6446$$aAnastasina, Maria$$b9
000164307 7001_ $$aSmura, Teemu$$b10
000164307 7001_ $$aLevanov, Lev$$b11
000164307 7001_ $$00000-0003-1528-044X$$aSzirovicza, Leonora$$b12
000164307 7001_ $$00000-0003-4797-5481$$aTobi, Allan$$b13
000164307 7001_ $$aKallio-Kokko, Hannimari$$b14
000164307 7001_ $$00000-0002-2229-6661$$aÖsterlund, Pamela$$b15
000164307 7001_ $$00000-0002-4533-0455$$aJoensuu, Merja$$b16
000164307 7001_ $$00000-0001-6400-1107$$aMeunier, Frédéric A$$b17
000164307 7001_ $$00000-0001-7060-5871$$aButcher, Sarah J$$b18
000164307 7001_ $$aWinkler, Martin Sebastian$$b19
000164307 7001_ $$0P:(DE-2719)9001340$$aMollenhauer, Brit$$b20
000164307 7001_ $$aHelenius, Ari$$b21
000164307 7001_ $$0P:(DE-2719)9002754$$aGökce, Ozgun$$b22$$udzne
000164307 7001_ $$00000-0002-9458-6385$$aTeesalu, Tambet$$b23
000164307 7001_ $$00000-0001-5699-214X$$aHepojoki, Jussi$$b24
000164307 7001_ $$00000-0003-2270-6824$$aVapalahti, Olli$$b25
000164307 7001_ $$0P:(DE-2719)9000922$$aStadelmann, Christine$$b26
000164307 7001_ $$00000-0002-3585-559X$$aBalistreri, Giuseppe$$b27
000164307 7001_ $$0P:(DE-2719)2811642$$aSimons, Mikael$$b28$$eLast author
000164307 773__ $$0PERI:(DE-600)2089761-3$$a10.1126/science.abd2985$$gVol. 370, no. 6518, p. 856 - 860$$n6518$$p856 - 860$$tScience / Science now$$v370$$x0036-8075$$y2020
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