TY  - JOUR
AU  - Cantuti-Castelvetri, Ludovico
AU  - Ojha, Ravi
AU  - Pedro, Liliana Domingues
AU  - Djannatian, Minou
AU  - Franz, Jonas
AU  - Kuivanen, Suvi
AU  - van der Meer, Franziska
AU  - Kallio, Katri
AU  - Kaya, Tugberk
AU  - Anastasina, Maria
AU  - Smura, Teemu
AU  - Levanov, Lev
AU  - Szirovicza, Leonora
AU  - Tobi, Allan
AU  - Kallio-Kokko, Hannimari
AU  - Österlund, Pamela
AU  - Joensuu, Merja
AU  - Meunier, Frédéric A
AU  - Butcher, Sarah J
AU  - Winkler, Martin Sebastian
AU  - Mollenhauer, Brit
AU  - Helenius, Ari
AU  - Gökce, Ozgun
AU  - Teesalu, Tambet
AU  - Hepojoki, Jussi
AU  - Vapalahti, Olli
AU  - Stadelmann, Christine
AU  - Balistreri, Giuseppe
AU  - Simons, Mikael
TI  - Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity.
JO  - Science / Science now
VL  - 370
IS  - 6518
SN  - 0036-8075
CY  - Washington, DC
PB  - Assoc.
M1  - DZNE-2022-00961
SP  - 856 - 860
PY  - 2020
N1  - ISSN 1095-9203 not unique: **3 hits**.
AB  - 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.
KW  - Angiotensin-Converting Enzyme 2
KW  - Animals
KW  - Antibodies, Monoclonal: immunology
KW  - Betacoronavirus: genetics
KW  - Betacoronavirus: physiology
KW  - COVID-19
KW  - Caco-2 Cells
KW  - Coronavirus Infections: virology
KW  - Female
KW  - HEK293 Cells
KW  - Host Microbial Interactions
KW  - Humans
KW  - Lung: metabolism
KW  - Male
KW  - Metal Nanoparticles
KW  - Mice
KW  - Mice, Inbred C57BL
KW  - Mutation
KW  - Neuropilin-1: chemistry
KW  - Neuropilin-1: genetics
KW  - Neuropilin-1: immunology
KW  - Neuropilin-1: metabolism
KW  - Neuropilin-2: metabolism
KW  - Olfactory Mucosa: metabolism
KW  - Olfactory Mucosa: virology
KW  - Pandemics
KW  - Peptide Fragments: metabolism
KW  - Peptidyl-Dipeptidase A: genetics
KW  - Peptidyl-Dipeptidase A: metabolism
KW  - Pneumonia, Viral: virology
KW  - Protein Binding
KW  - Protein Domains
KW  - Respiratory Mucosa: metabolism
KW  - SARS-CoV-2
KW  - Serine Endopeptidases: genetics
KW  - Serine Endopeptidases: metabolism
KW  - Spike Glycoprotein, Coronavirus: chemistry
KW  - Spike Glycoprotein, Coronavirus: metabolism
KW  - Virus Internalization
KW  - Antibodies, Monoclonal (NLM Chemicals)
KW  - NRP1 protein, human (NLM Chemicals)
KW  - Neuropilin-2 (NLM Chemicals)
KW  - Peptide Fragments (NLM Chemicals)
KW  - Spike Glycoprotein, Coronavirus (NLM Chemicals)
KW  - neuropilin-2, human (NLM Chemicals)
KW  - spike protein, SARS-CoV-2 (NLM Chemicals)
KW  - Neuropilin-1 (NLM Chemicals)
KW  - Peptidyl-Dipeptidase A (NLM Chemicals)
KW  - ACE2 protein, human (NLM Chemicals)
KW  - Ace2 protein, mouse (NLM Chemicals)
KW  - Angiotensin-Converting Enzyme 2 (NLM Chemicals)
KW  - Serine Endopeptidases (NLM Chemicals)
KW  - TMPRSS2 protein, human (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:33082293
C2  - pmc:PMC7857391
DO  - DOI:10.1126/science.abd2985
UR  - https://pub.dzne.de/record/164307
ER  -