Roles of spike protein in the pathogenesis of SARS coronavirus.
Identifieur interne : 001829 ( PubMed/Curation ); précédent : 001828; suivant : 001830Roles of spike protein in the pathogenesis of SARS coronavirus.
Auteurs : D Y Jin [République populaire de Chine] ; B J ZhengSource :
- Hong Kong medical journal = Xianggang yi xue za zhi [ 1024-2708 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Cellules Vero, Cellules cultivées, Facteur Xa (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Inhibiteurs de protéases (pharmacologie), Pliage des protéines (), Protéines de l'enveloppe virale (métabolisme), Pénétration virale (), Syndrome respiratoire aigu sévère (), Systèmes de délivrance de médicaments, Virus du SRAS (), Virus du SRAS (métabolisme), eIF-2 Kinase (métabolisme).
- MESH :
- métabolisme : Facteur Xa, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus du SRAS, eIF-2 Kinase.
- pharmacologie : Inhibiteurs de protéases.
- Animaux, Cellules Vero, Cellules cultivées, Glycoprotéine de spicule des coronavirus, Pliage des protéines, Pénétration virale, Syndrome respiratoire aigu sévère, Systèmes de délivrance de médicaments, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Cells, Cultured, Chlorocebus aethiops, Drug Delivery Systems, Factor Xa (metabolism), Membrane Glycoproteins (metabolism), Protease Inhibitors (pharmacology), Protein Folding (drug effects), SARS Virus (drug effects), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (prevention & control), Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (metabolism), Virus Internalization (drug effects), eIF-2 Kinase (metabolism).
- MESH :
- chemical , metabolism : Factor Xa, Membrane Glycoproteins, Viral Envelope Proteins, eIF-2 Kinase.
- chemical , pharmacology : Protease Inhibitors.
- drug effects : Protein Folding, SARS Virus, Virus Internalization.
- metabolism : SARS Virus.
- prevention & control : Severe Acute Respiratory Syndrome.
- Animals, Cells, Cultured, Chlorocebus aethiops, Drug Delivery Systems, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
1. Infection with SARS coronavirus (SARS-CoV) induces a cellular stress condition known as the unfolded protein response (UPR). UPR induction is mediated primarily by viral spike (S) protein. The modulation of UPR by S protein involves activation of PERK protein kinase. Other branches of the UPR pathways controlled by IRE1 and ATF6 proteins, respectively, are not involved. 2. The protease inhibitor Ben-HCl effectively suppresses SARS-CoV infection by blocking virus entry. Viral infectivity is associated with the cleavage of S protein by the cellular protease factor Xa. 3. Two new aspects of the interaction between SARS-CoV S protein and the cell have been defined. These have important implications in the pathogenesis of SARS, providing opportunities for developing vaccines and antivirals against SARS-CoV. 4. Counteracting the UPR and targeting the cleavage of S protein with small molecule pharmaceutical agents represent two new anti-SARS-CoV strategies. 5. The receptor-binding domain of S protein delivered via adeno-associated virus can efficiently induce mucosal immunity and provide long-term protection against SARS-CoV infection.
PubMed: 19258633
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pubmed:19258633Le document en format XML
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<affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, The University of Hong Kong, 21 Sassoon Road, Hong Kong SAR, China. dyjin@ hkucc.hku.hk</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Department of Biochemistry, The University of Hong Kong, 21 Sassoon Road, Hong Kong SAR</wicri:regionArea>
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<author><name sortKey="Zheng, B J" sort="Zheng, B J" uniqKey="Zheng B" first="B J" last="Zheng">B J Zheng</name>
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<term>Factor Xa (metabolism)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Protease Inhibitors (pharmacology)</term>
<term>Protein Folding (drug effects)</term>
<term>SARS Virus (drug effects)</term>
<term>SARS Virus (metabolism)</term>
<term>Severe Acute Respiratory Syndrome (prevention & control)</term>
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<term>Cellules cultivées</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
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<term>Pliage des protéines ()</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
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<term>Syndrome respiratoire aigu sévère ()</term>
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<term>Virus du SRAS (métabolisme)</term>
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<term>eIF-2 Kinase</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Protease Inhibitors</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Protein Folding</term>
<term>SARS Virus</term>
<term>Virus Internalization</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term>
</keywords>
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<term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Virus du SRAS</term>
<term>eIF-2 Kinase</term>
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<term>Cells, Cultured</term>
<term>Chlorocebus aethiops</term>
<term>Drug Delivery Systems</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Vero Cells</term>
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<term>Cellules Vero</term>
<term>Cellules cultivées</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Pliage des protéines</term>
<term>Pénétration virale</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Systèmes de délivrance de médicaments</term>
<term>Virus du SRAS</term>
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<front><div type="abstract" xml:lang="en">1. Infection with SARS coronavirus (SARS-CoV) induces a cellular stress condition known as the unfolded protein response (UPR). UPR induction is mediated primarily by viral spike (S) protein. The modulation of UPR by S protein involves activation of PERK protein kinase. Other branches of the UPR pathways controlled by IRE1 and ATF6 proteins, respectively, are not involved. 2. The protease inhibitor Ben-HCl effectively suppresses SARS-CoV infection by blocking virus entry. Viral infectivity is associated with the cleavage of S protein by the cellular protease factor Xa. 3. Two new aspects of the interaction between SARS-CoV S protein and the cell have been defined. These have important implications in the pathogenesis of SARS, providing opportunities for developing vaccines and antivirals against SARS-CoV. 4. Counteracting the UPR and targeting the cleavage of S protein with small molecule pharmaceutical agents represent two new anti-SARS-CoV strategies. 5. The receptor-binding domain of S protein delivered via adeno-associated virus can efficiently induce mucosal immunity and provide long-term protection against SARS-CoV infection.</div>
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<Abstract><AbstractText>1. Infection with SARS coronavirus (SARS-CoV) induces a cellular stress condition known as the unfolded protein response (UPR). UPR induction is mediated primarily by viral spike (S) protein. The modulation of UPR by S protein involves activation of PERK protein kinase. Other branches of the UPR pathways controlled by IRE1 and ATF6 proteins, respectively, are not involved. 2. The protease inhibitor Ben-HCl effectively suppresses SARS-CoV infection by blocking virus entry. Viral infectivity is associated with the cleavage of S protein by the cellular protease factor Xa. 3. Two new aspects of the interaction between SARS-CoV S protein and the cell have been defined. These have important implications in the pathogenesis of SARS, providing opportunities for developing vaccines and antivirals against SARS-CoV. 4. Counteracting the UPR and targeting the cleavage of S protein with small molecule pharmaceutical agents represent two new anti-SARS-CoV strategies. 5. The receptor-binding domain of S protein delivered via adeno-associated virus can efficiently induce mucosal immunity and provide long-term protection against SARS-CoV infection.</AbstractText>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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