Receptor variation and susceptibility to Middle East respiratory syndrome coronavirus infection.
Identifieur interne : 001B07 ( Main/Exploration ); précédent : 001B06; suivant : 001B08Receptor variation and susceptibility to Middle East respiratory syndrome coronavirus infection.
Auteurs : Arlene Barlan [États-Unis] ; Jincun Zhao ; Mayukh K. Sarkar ; Kun Li ; Paul B. Mccray ; Stanley Perlman ; Tom GallagherSource :
- Journal of virology [ 1098-5514 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, Animaux domestiques, Animaux sauvages, Attachement viral, Coronavirus (physiologie), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Liaison aux protéines, Peptide hydrolases (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéolyse, Récepteurs viraux (génétique), Récepteurs viraux (métabolisme), Variation génétique.
- MESH :
- génétique : Protéines recombinantes, Récepteurs viraux.
- métabolisme : Glycoprotéine de spicule des coronavirus, Peptide hydrolases, Protéines recombinantes, Récepteurs viraux.
- physiologie : Coronavirus.
- Animaux, Animaux domestiques, Animaux sauvages, Attachement viral, Humains, Liaison aux protéines, Protéolyse, Variation génétique.
English descriptors
- KwdEn :
- Animals, Animals, Domestic, Animals, Wild, Coronavirus (physiology), Genetic Variation, Humans, Peptide Hydrolases (metabolism), Protein Binding, Proteolysis, Receptors, Virus (genetics), Receptors, Virus (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Spike Glycoprotein, Coronavirus (metabolism), Virus Attachment.
- MESH :
- chemical , genetics : Receptors, Virus, Recombinant Proteins.
- chemical , metabolism : Peptide Hydrolases, Receptors, Virus, Recombinant Proteins, Spike Glycoprotein, Coronavirus.
- physiology : Coronavirus.
- Animals, Animals, Domestic, Animals, Wild, Genetic Variation, Humans, Protein Binding, Proteolysis, Virus Attachment.
Abstract
The Middle East respiratory syndrome coronavirus (MERS-CoV) recently spread from an animal reservoir to infect humans, causing sporadic severe and frequently fatal respiratory disease. Appropriate public health and control measures will require discovery of the zoonotic MERS coronavirus reservoirs. The relevant animal hosts are liable to be those that offer optimal MERS virus cell entry. Cell entry begins with virus spike (S) protein binding to DPP4 receptors. We constructed chimeric DPP4 receptors that have the virus-binding domains of indigenous Middle Eastern animals and assessed the activities of these receptors in supporting S protein binding and virus entry. Human, camel, and horse receptors were potent and nearly equally effective MERS virus receptors, while goat and bat receptors were considerably less effective. These patterns reflected S protein affinities for the receptors. However, even the low-affinity receptors could hypersensitize cells to infection when an S-cleaving protease(s) was present, indicating that affinity thresholds for virus entry must be considered in the context of host-cell proteolytic environments. These findings suggest that virus receptors and S protein-cleaving proteases combine in a variety of animals to offer efficient virus entry and that several Middle Eastern animals are potential reservoirs for transmitting MERS-CoV to humans.
DOI: 10.1128/JVI.00161-14
PubMed: 24554656
Affiliations:
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Le document en format XML
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Sarkar</name></author><author><name sortKey="Li, Kun" sort="Li, Kun" uniqKey="Li K" first="Kun" last="Li">Kun Li</name></author><author><name sortKey="Mccray, Paul B" sort="Mccray, Paul B" uniqKey="Mccray P" first="Paul B" last="Mccray">Paul B. Mccray</name></author><author><name sortKey="Perlman, Stanley" sort="Perlman, Stanley" uniqKey="Perlman S" first="Stanley" last="Perlman">Stanley Perlman</name></author><author><name sortKey="Gallagher, Tom" sort="Gallagher, Tom" uniqKey="Gallagher T" first="Tom" last="Gallagher">Tom Gallagher</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Animals, Domestic</term><term>Animals, Wild</term><term>Coronavirus (physiology)</term><term>Genetic Variation</term><term>Humans</term><term>Peptide Hydrolases (metabolism)</term><term>Protein Binding</term><term>Proteolysis</term><term>Receptors, Virus (genetics)</term><term>Receptors, Virus (metabolism)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Virus Attachment</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Animaux domestiques</term><term>Animaux sauvages</term><term>Attachement viral</term><term>Coronavirus (physiologie)</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Peptide hydrolases (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéolyse</term><term>Récepteurs viraux (génétique)</term><term>Récepteurs viraux (métabolisme)</term><term>Variation génétique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Receptors, Virus</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Hydrolases</term><term>Receptors, Virus</term><term>Recombinant Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines recombinantes</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term><term>Peptide hydrolases</term><term>Protéines recombinantes</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Animals, Domestic</term><term>Animals, Wild</term><term>Genetic Variation</term><term>Humans</term><term>Protein Binding</term><term>Proteolysis</term><term>Virus Attachment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Animaux domestiques</term><term>Animaux sauvages</term><term>Attachement viral</term><term>Humains</term><term>Liaison aux protéines</term><term>Protéolyse</term><term>Variation génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Middle East respiratory syndrome coronavirus (MERS-CoV) recently spread from an animal reservoir to infect humans, causing sporadic severe and frequently fatal respiratory disease. Appropriate public health and control measures will require discovery of the zoonotic MERS coronavirus reservoirs. The relevant animal hosts are liable to be those that offer optimal MERS virus cell entry. Cell entry begins with virus spike (S) protein binding to DPP4 receptors. We constructed chimeric DPP4 receptors that have the virus-binding domains of indigenous Middle Eastern animals and assessed the activities of these receptors in supporting S protein binding and virus entry. Human, camel, and horse receptors were potent and nearly equally effective MERS virus receptors, while goat and bat receptors were considerably less effective. These patterns reflected S protein affinities for the receptors. However, even the low-affinity receptors could hypersensitize cells to infection when an S-cleaving protease(s) was present, indicating that affinity thresholds for virus entry must be considered in the context of host-cell proteolytic environments. These findings suggest that virus receptors and S protein-cleaving proteases combine in a variety of animals to offer efficient virus entry and that several Middle Eastern animals are potential reservoirs for transmitting MERS-CoV to humans.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Illinois</li></region></list><tree><noCountry><name sortKey="Gallagher, Tom" sort="Gallagher, Tom" uniqKey="Gallagher T" first="Tom" last="Gallagher">Tom Gallagher</name><name sortKey="Li, Kun" sort="Li, Kun" uniqKey="Li K" first="Kun" last="Li">Kun Li</name><name sortKey="Mccray, Paul B" sort="Mccray, Paul B" uniqKey="Mccray P" first="Paul B" last="Mccray">Paul B. Mccray</name><name sortKey="Perlman, Stanley" sort="Perlman, Stanley" uniqKey="Perlman S" first="Stanley" last="Perlman">Stanley Perlman</name><name sortKey="Sarkar, Mayukh K" sort="Sarkar, Mayukh K" uniqKey="Sarkar M" first="Mayukh K" last="Sarkar">Mayukh K. Sarkar</name><name sortKey="Zhao, Jincun" sort="Zhao, Jincun" uniqKey="Zhao J" first="Jincun" last="Zhao">Jincun Zhao</name></noCountry><country name="États-Unis"><region name="Illinois"><name sortKey="Barlan, Arlene" sort="Barlan, Arlene" uniqKey="Barlan A" first="Arlene" last="Barlan">Arlene Barlan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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