Characterization of the spike protein of human coronavirus NL63 in receptor binding and pseudotype virus entry.
Identifieur interne : 002368 ( Ncbi/Curation ); précédent : 002367; suivant : 002369Characterization of the spike protein of human coronavirus NL63 in receptor binding and pseudotype virus entry.
Auteurs : Han-Xin Lin [Canada] ; Yan Feng ; Xinming Tu ; Xuesen Zhao ; Chih-Heng Hsieh ; Lauren Griffin ; Murray Junop ; Chengsheng ZhangSource :
- Virus research [ 1872-7492 ] ; 2011.
Descripteurs français
- KwdFr :
- Coronavirus humain NL63 (génétique), Coronavirus humain NL63 (physiologie), Délétion de séquence, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Humains, Liaison aux protéines, Lignée cellulaire, Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines mutantes (génétique), Protéines mutantes (métabolisme), Pénétration virale, Récepteurs viraux (métabolisme), Substitution d'acide aminé.
- MESH :
- génétique : Coronavirus humain NL63, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines mutantes.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines mutantes, Récepteurs viraux.
- physiologie : Coronavirus humain NL63.
- Délétion de séquence, Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Lignée cellulaire, Pénétration virale, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution, Cell Line, Coronavirus NL63, Human (genetics), Coronavirus NL63, Human (physiology), Humans, Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mutant Proteins (genetics), Mutant Proteins (metabolism), Protein Binding, Receptors, Virus (metabolism), Sequence Deletion, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virus Internalization.
- MESH :
- chemical , genetics : Membrane Glycoproteins, Mutant Proteins, Viral Envelope Proteins.
- genetics : Coronavirus NL63, Human.
- chemical , metabolism : Membrane Glycoproteins, Mutant Proteins, Receptors, Virus, Viral Envelope Proteins.
- physiology : Coronavirus NL63, Human.
- Amino Acid Substitution, Cell Line, Humans, Protein Binding, Sequence Deletion, Spike Glycoprotein, Coronavirus, Virus Internalization.
Abstract
The spike (S) protein of human coronavirus NL63 (HCoV-NL63) mediates both cell attachment by binding to its receptor hACE2 and membrane fusion during virus entry. We have previously identified the receptor-binding domain (RBD) and residues important for RBD-hACE2 association. Here, we further characterized the S protein by investigating the roles of the cytoplasmic tail and 19 residues located in the RBD in protein accumulation, receptor binding, and pseudotype virus entry. For these purposes, we first identified an entry-efficient S gene template from a pool of gene variants and used it as a backbone to generate a series of cytoplasmic tail deletion and single residue substitution mutants. Our results showed that: (i) deletion of 18aa from the C-terminus enhanced the S protein accumulation and virus entry, which might be due to the deletion of intracellular retention signals; (ii) further deletion to residue 29 also enhanced the amount of S protein on the cell surface and in virion, but reduced virus entry by 25%, suggesting that residues 19-29 contributes to membrane fusion; (iii) a 29aa-deletion mutant had a defect in anchoring on the plasma membrane, which led to a dramatic decrease of S protein in virion and virus entry; (iv) a total of 15 residues (Y498, V499, V531, G534, G537, D538, S540, G575, S576, E582, W585, Y590, T591, V593 and G594) within RBD were important for receptor binding and virus entry. They probably form three receptor binding motifs, and the third motif is conserved between NL63 and SARS-CoV.
DOI: 10.1016/j.virusres.2011.06.029
PubMed: 21798295
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Tu</name></author><author><name sortKey="Zhao, Xuesen" sort="Zhao, Xuesen" uniqKey="Zhao X" first="Xuesen" last="Zhao">Xuesen Zhao</name></author><author><name sortKey="Hsieh, Chih Heng" sort="Hsieh, Chih Heng" uniqKey="Hsieh C" first="Chih-Heng" last="Hsieh">Chih-Heng Hsieh</name></author><author><name sortKey="Griffin, Lauren" sort="Griffin, Lauren" uniqKey="Griffin L" first="Lauren" last="Griffin">Lauren Griffin</name></author><author><name sortKey="Junop, Murray" sort="Junop, Murray" uniqKey="Junop M" first="Murray" last="Junop">Murray Junop</name></author><author><name sortKey="Zhang, Chengsheng" sort="Zhang, Chengsheng" uniqKey="Zhang C" first="Chengsheng" last="Zhang">Chengsheng Zhang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21798295</idno><idno type="pmid">21798295</idno><idno type="doi">10.1016/j.virusres.2011.06.029</idno><idno type="wicri:Area/PubMed/Corpus">001487</idno><idno 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of Pathology and Molecular Medicine, McMaster University</wicri:regionArea><placeName><settlement type="city">Hamilton (Ontario)</settlement><region type="state">Ontario</region></placeName><orgName type="university">Université McMaster</orgName></affiliation></author><author><name sortKey="Feng, Yan" sort="Feng, Yan" uniqKey="Feng Y" first="Yan" last="Feng">Yan Feng</name></author><author><name sortKey="Tu, Xinming" sort="Tu, Xinming" uniqKey="Tu X" first="Xinming" last="Tu">Xinming Tu</name></author><author><name sortKey="Zhao, Xuesen" sort="Zhao, Xuesen" uniqKey="Zhao X" first="Xuesen" last="Zhao">Xuesen Zhao</name></author><author><name sortKey="Hsieh, Chih Heng" sort="Hsieh, Chih Heng" uniqKey="Hsieh C" first="Chih-Heng" last="Hsieh">Chih-Heng Hsieh</name></author><author><name sortKey="Griffin, Lauren" sort="Griffin, Lauren" uniqKey="Griffin L" first="Lauren" last="Griffin">Lauren Griffin</name></author><author><name sortKey="Junop, Murray" sort="Junop, Murray" uniqKey="Junop M" first="Murray" last="Junop">Murray Junop</name></author><author><name sortKey="Zhang, Chengsheng" sort="Zhang, Chengsheng" uniqKey="Zhang C" first="Chengsheng" last="Zhang">Chengsheng Zhang</name></author></analytic><series><title level="j">Virus research</title><idno type="eISSN">1872-7492</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>Cell Line</term><term>Coronavirus NL63, Human (genetics)</term><term>Coronavirus NL63, Human (physiology)</term><term>Humans</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mutant Proteins (genetics)</term><term>Mutant Proteins (metabolism)</term><term>Protein Binding</term><term>Receptors, Virus (metabolism)</term><term>Sequence Deletion</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Coronavirus humain NL63 (génétique)</term><term>Coronavirus humain NL63 (physiologie)</term><term>Délétion de séquence</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéines mutantes (génétique)</term><term>Protéines mutantes (métabolisme)</term><term>Pénétration virale</term><term>Récepteurs viraux (métabolisme)</term><term>Substitution d'acide aminé</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Mutant Proteins</term><term>Viral 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Human</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Cell Line</term><term>Humans</term><term>Protein Binding</term><term>Sequence Deletion</term><term>Spike Glycoprotein, Coronavirus</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Délétion de séquence</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Pénétration virale</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The spike (S) protein of human coronavirus NL63 (HCoV-NL63) mediates both cell attachment by binding to its receptor hACE2 and membrane fusion during virus entry. We have previously identified the receptor-binding domain (RBD) and residues important for RBD-hACE2 association. Here, we further characterized the S protein by investigating the roles of the cytoplasmic tail and 19 residues located in the RBD in protein accumulation, receptor binding, and pseudotype virus entry. For these purposes, we first identified an entry-efficient S gene template from a pool of gene variants and used it as a backbone to generate a series of cytoplasmic tail deletion and single residue substitution mutants. Our results showed that: (i) deletion of 18aa from the C-terminus enhanced the S protein accumulation and virus entry, which might be due to the deletion of intracellular retention signals; (ii) further deletion to residue 29 also enhanced the amount of S protein on the cell surface and in virion, but reduced virus entry by 25%, suggesting that residues 19-29 contributes to membrane fusion; (iii) a 29aa-deletion mutant had a defect in anchoring on the plasma membrane, which led to a dramatic decrease of S protein in virion and virus entry; (iv) a total of 15 residues (Y498, V499, V531, G534, G537, D538, S540, G575, S576, E582, W585, Y590, T591, V593 and G594) within RBD were important for receptor binding and virus entry. They probably form three receptor binding motifs, and the third motif is conserved between NL63 and SARS-CoV.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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