Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses.
Identifieur interne : 000619 ( Main/Exploration ); précédent : 000618; suivant : 000620Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses.
Auteurs : Michael Letko [États-Unis] ; Andrea Marzi [États-Unis] ; Vincent Munster [États-Unis]Source :
- Nature microbiology [ 2058-5276 ] ; 2020.
Descripteurs français
- KwdFr :
- Animaux, Dipeptidyl peptidase 4 (métabolisme), Domaines protéiques, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Infections à coronavirus (métabolisme), Infections à coronavirus (virologie), Lignée cellulaire, Mutation, Pandémies, Peptidyl-Dipeptidase A (), Peptidyl-Dipeptidase A (génétique), Peptidyl-Dipeptidase A (métabolisme), Pneumopathie virale (métabolisme), Pneumopathie virale (virologie), Protéines de fusion recombinantes (métabolisme), Pénétration virale, Récepteurs viraux (), Récepteurs viraux (génétique), Récepteurs viraux (métabolisme), Trypsine (métabolisme), Virus du SRAS (), Virus du SRAS (physiologie).
- MESH :
- génétique : Glycoprotéine de spicule des coronavirus, Peptidyl-Dipeptidase A, Récepteurs viraux.
- métabolisme : Dipeptidyl peptidase 4, Glycoprotéine de spicule des coronavirus, Infections à coronavirus, Peptidyl-Dipeptidase A, Pneumopathie virale, Protéines de fusion recombinantes, Récepteurs viraux, Trypsine.
- physiologie : Virus du SRAS.
- virologie : Infections à coronavirus, Pneumopathie virale.
- Animaux, Domaines protéiques, Glycoprotéine de spicule des coronavirus, Humains, Lignée cellulaire, Mutation, Pandémies, Peptidyl-Dipeptidase A, Pénétration virale, Récepteurs viraux, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Betacoronavirus (chemistry), Betacoronavirus (classification), Betacoronavirus (physiology), CD13 Antigens (metabolism), Cell Line, Coronavirus Infections (metabolism), Coronavirus Infections (virology), Dipeptidyl Peptidase 4 (metabolism), Humans, Mutation, Pandemics, Peptidyl-Dipeptidase A (chemistry), Peptidyl-Dipeptidase A (genetics), Peptidyl-Dipeptidase A (metabolism), Pneumonia, Viral (metabolism), Pneumonia, Viral (virology), Protein Domains, Receptors, Virus (chemistry), Receptors, Virus (genetics), Receptors, Virus (metabolism), Recombinant Fusion Proteins (metabolism), SARS Virus (chemistry), SARS Virus (physiology), Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Trypsin (metabolism), Virus Internalization.
- MESH :
- chemical , chemistry : Peptidyl-Dipeptidase A, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemical , genetics : Peptidyl-Dipeptidase A, Receptors, Virus, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : CD13 Antigens, Dipeptidyl Peptidase 4, Peptidyl-Dipeptidase A, Receptors, Virus, Recombinant Fusion Proteins, Spike Glycoprotein, Coronavirus, Trypsin.
- chemistry : Betacoronavirus, SARS Virus.
- classification : Betacoronavirus.
- metabolism : Coronavirus Infections, Pneumonia, Viral.
- physiology : Betacoronavirus, SARS Virus.
- virology : Coronavirus Infections, Pneumonia, Viral.
- Animals, Cell Line, Humans, Mutation, Pandemics, Protein Domains, Virus Internalization.
Abstract
Over the past 20 years, several coronaviruses have crossed the species barrier into humans, causing outbreaks of severe, and often fatal, respiratory illness. Since SARS-CoV was first identified in animal markets, global viromics projects have discovered thousands of coronavirus sequences in diverse animals and geographic regions. Unfortunately, there are few tools available to functionally test these viruses for their ability to infect humans, which has severely hampered efforts to predict the next zoonotic viral outbreak. Here, we developed an approach to rapidly screen lineage B betacoronaviruses, such as SARS-CoV and the recent SARS-CoV-2, for receptor usage and their ability to infect cell types from different species. We show that host protease processing during viral entry is a significant barrier for several lineage B viruses and that bypassing this barrier allows several lineage B viruses to enter human cells through an unknown receptor. We also demonstrate how different lineage B viruses can recombine to gain entry into human cells, and confirm that human ACE2 is the receptor for the recently emerging SARS-CoV-2.
DOI: 10.1038/s41564-020-0688-y
PubMed: 32094589
Affiliations:
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Le document en format XML
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wicri:level="2"><nlm:affiliation>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT, USA. vincent.munster@nih.gov.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation></author></analytic><series><title level="j">Nature microbiology</title><idno type="eISSN">2058-5276</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Betacoronavirus (chemistry)</term><term>Betacoronavirus (classification)</term><term>Betacoronavirus (physiology)</term><term>CD13 Antigens (metabolism)</term><term>Cell Line</term><term>Coronavirus Infections (metabolism)</term><term>Coronavirus Infections (virology)</term><term>Dipeptidyl Peptidase 4 (metabolism)</term><term>Humans</term><term>Mutation</term><term>Pandemics</term><term>Peptidyl-Dipeptidase A (chemistry)</term><term>Peptidyl-Dipeptidase A (genetics)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Pneumonia, Viral (metabolism)</term><term>Pneumonia, Viral (virology)</term><term>Protein Domains</term><term>Receptors, Virus (chemistry)</term><term>Receptors, Virus (genetics)</term><term>Receptors, Virus (metabolism)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (genetics)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Trypsin (metabolism)</term><term>Virus Internalization</term></keywords><keywords 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()</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>CD13 Antigens</term><term>Dipeptidyl Peptidase 4</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Recombinant Fusion Proteins</term><term>Spike Glycoprotein, Coronavirus</term><term>Trypsin</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Betacoronavirus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="en"><term>Betacoronavirus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term><term>Peptidyl-Dipeptidase A</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus Infections</term><term>Pneumonia, Viral</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dipeptidyl peptidase 4</term><term>Glycoprotéine de spicule des coronavirus</term><term>Infections à coronavirus</term><term>Peptidyl-Dipeptidase A</term><term>Pneumopathie virale</term><term>Protéines de fusion recombinantes</term><term>Récepteurs viraux</term><term>Trypsine</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Betacoronavirus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à coronavirus</term><term>Pneumopathie virale</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term><term>Pneumonia, Viral</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Mutation</term><term>Pandemics</term><term>Protein Domains</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Domaines protéiques</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Lignée cellulaire</term><term>Mutation</term><term>Pandémies</term><term>Peptidyl-Dipeptidase A</term><term>Pénétration virale</term><term>Récepteurs viraux</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Over the past 20 years, several coronaviruses have crossed the species barrier into humans, causing outbreaks of severe, and often fatal, respiratory illness. Since SARS-CoV was first identified in animal markets, global viromics projects have discovered thousands of coronavirus sequences in diverse animals and geographic regions. Unfortunately, there are few tools available to functionally test these viruses for their ability to infect humans, which has severely hampered efforts to predict the next zoonotic viral outbreak. Here, we developed an approach to rapidly screen lineage B betacoronaviruses, such as SARS-CoV and the recent SARS-CoV-2, for receptor usage and their ability to infect cell types from different species. We show that host protease processing during viral entry is a significant barrier for several lineage B viruses and that bypassing this barrier allows several lineage B viruses to enter human cells through an unknown receptor. We also demonstrate how different lineage B viruses can recombine to gain entry into human cells, and confirm that human ACE2 is the receptor for the recently emerging SARS-CoV-2.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Montana</li></region></list><tree><country name="États-Unis"><region name="Montana"><name sortKey="Letko, Michael" sort="Letko, Michael" uniqKey="Letko M" first="Michael" last="Letko">Michael Letko</name></region><name sortKey="Marzi, Andrea" sort="Marzi, Andrea" uniqKey="Marzi A" first="Andrea" last="Marzi">Andrea Marzi</name><name sortKey="Munster, Vincent" sort="Munster, Vincent" uniqKey="Munster V" first="Vincent" last="Munster">Vincent Munster</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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