%0 Journal Article
%A Cantuti-Castelvetri, Ludovico
%A Ojha, Ravi
%A Pedro, Liliana Domingues
%A Djannatian, Minou
%A Franz, Jonas
%A Kuivanen, Suvi
%A van der Meer, Franziska
%A Kallio, Katri
%A Kaya, Tugberk
%A Anastasina, Maria
%A Smura, Teemu
%A Levanov, Lev
%A Szirovicza, Leonora
%A Tobi, Allan
%A Kallio-Kokko, Hannimari
%A Österlund, Pamela
%A Joensuu, Merja
%A Meunier, Frédéric A
%A Butcher, Sarah J
%A Winkler, Martin Sebastian
%A Mollenhauer, Brit
%A Helenius, Ari
%A Gökce, Ozgun
%A Teesalu, Tambet
%A Hepojoki, Jussi
%A Vapalahti, Olli
%A Stadelmann, Christine
%A Balistreri, Giuseppe
%A Simons, Mikael
%T Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity.
%J Science / Science now
%V 370
%N 6518
%@ 0036-8075
%C Washington, DC
%I Assoc.
%M DZNE-2022-00961
%P 856 - 860
%D 2020
%Z ISSN 1095-9203 not unique: **3 hits**.
%X 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.
%K Angiotensin-Converting Enzyme 2
%K Animals
%K Antibodies, Monoclonal: immunology
%K Betacoronavirus: genetics
%K Betacoronavirus: physiology
%K COVID-19
%K Caco-2 Cells
%K Coronavirus Infections: virology
%K Female
%K HEK293 Cells
%K Host Microbial Interactions
%K Humans
%K Lung: metabolism
%K Male
%K Metal Nanoparticles
%K Mice
%K Mice, Inbred C57BL
%K Mutation
%K Neuropilin-1: chemistry
%K Neuropilin-1: genetics
%K Neuropilin-1: immunology
%K Neuropilin-1: metabolism
%K Neuropilin-2: metabolism
%K Olfactory Mucosa: metabolism
%K Olfactory Mucosa: virology
%K Pandemics
%K Peptide Fragments: metabolism
%K Peptidyl-Dipeptidase A: genetics
%K Peptidyl-Dipeptidase A: metabolism
%K Pneumonia, Viral: virology
%K Protein Binding
%K Protein Domains
%K Respiratory Mucosa: metabolism
%K SARS-CoV-2
%K Serine Endopeptidases: genetics
%K Serine Endopeptidases: metabolism
%K Spike Glycoprotein, Coronavirus: chemistry
%K Spike Glycoprotein, Coronavirus: metabolism
%K Virus Internalization
%K Antibodies, Monoclonal (NLM Chemicals)
%K NRP1 protein, human (NLM Chemicals)
%K Neuropilin-2 (NLM Chemicals)
%K Peptide Fragments (NLM Chemicals)
%K Spike Glycoprotein, Coronavirus (NLM Chemicals)
%K neuropilin-2, human (NLM Chemicals)
%K spike protein, SARS-CoV-2 (NLM Chemicals)
%K Neuropilin-1 (NLM Chemicals)
%K Peptidyl-Dipeptidase A (NLM Chemicals)
%K ACE2 protein, human (NLM Chemicals)
%K Ace2 protein, mouse (NLM Chemicals)
%K Angiotensin-Converting Enzyme 2 (NLM Chemicals)
%K Serine Endopeptidases (NLM Chemicals)
%K TMPRSS2 protein, human (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:33082293
%2 pmc:PMC7857391
%R 10.1126/science.abd2985
%U https://pub.dzne.de/record/164307