Expression, glycosylation, and modification of the spike (S) glycoprotein of SARS CoV.
Identifieur interne : 001962 ( Ncbi/Merge ); précédent : 001961; suivant : 001963Expression, glycosylation, and modification of the spike (S) glycoprotein of SARS CoV.
Auteurs : Shuo Shen [Singapour] ; Timothy H P. Tan ; Yee-Joo TanSource :
- Methods in molecular biology (Clifton, N.J.) [ 1064-3745 ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux, Cellules COS, Cellules Vero, Expression des gènes, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (analyse), Glycoprotéines membranaires (biosynthèse), Glycoprotéines membranaires (génétique), Glycosylation, Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase (), Modification traductionnelle des protéines (physiologie), Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (), Protéines de l'enveloppe virale (analyse), Protéines de l'enveloppe virale (biosynthèse), Protéines de l'enveloppe virale (génétique), Protéines recombinantes (analyse), Protéines recombinantes (biosynthèse), Protéines recombinantes (génétique), Virus de la vaccine (génétique), Virus du SRAS (génétique).
- MESH :
- analyse : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes.
- biosynthèse : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes.
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes, Virus de la vaccine, Virus du SRAS.
- physiologie : Modification traductionnelle des protéines.
- Animaux, Cellules COS, Cellules Vero, Expression des gènes, Glycoprotéine de spicule des coronavirus, Glycosylation, Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase, Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase.
English descriptors
- KwdEn :
- Animals, COS Cells, Chlorocebus aethiops, Gene Expression, Glycosylation, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase (chemistry), Membrane Glycoproteins (analysis), Membrane Glycoproteins (biosynthesis), Membrane Glycoproteins (genetics), Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (chemistry), Protein Modification, Translational (physiology), Recombinant Proteins (analysis), Recombinant Proteins (biosynthesis), Recombinant Proteins (genetics), SARS Virus (genetics), Spike Glycoprotein, Coronavirus, Vaccinia virus (genetics), Vero Cells, Viral Envelope Proteins (analysis), Viral Envelope Proteins (biosynthesis), Viral Envelope Proteins (genetics).
- MESH :
- chemical , analysis : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , biosynthesis : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , chemistry : Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase.
- chemical , genetics : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- genetics : SARS Virus, Vaccinia virus.
- physiology : Protein Modification, Translational.
- Animals, COS Cells, Chlorocebus aethiops, Gene Expression, Glycosylation, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. To study the maturation pathway of the S glycoprotein of the severe acute respiratory syndrome (SARS)-coronavirus (CoV) within the host cell, a T7/vaccinia virus-based expression system coupled to immunoprecipitation with anti-S antibodies was used to test and analyze different forms of the S glycoprotein. The state of maturity of the S glycoprotein can be deduced from its sensitivity to hydrolysis by endoglycosidase H (EndoH) or N-glycosidase F (N-Gly F). A fully matured S glycoprotein will be modified with complex oligosaccharides which makes it resistant to cleavage by EndoH but not by N-Gly F. By exploiting this characteristic, it is then possible to determine which forms of the immunoprecipitated S protein are properly processed by the host cell. With this system, many different constructs of the S glycoprotein can be analyzed in parallel thus providing another method by which to study the functional domains of S involved in membrane fusion event that occurs during viral infection.
DOI: 10.1007/978-1-59745-393-6_9
PubMed: 17502675
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(analyse)</term><term>Protéines de l'enveloppe virale (biosynthèse)</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines recombinantes (analyse)</term><term>Protéines recombinantes (biosynthèse)</term><term>Protéines recombinantes (génétique)</term><term>Virus de la vaccine (génétique)</term><term>Virus du SRAS (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase</term><term>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term><term>Vaccinia virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term><term>Virus de la vaccine</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Modification 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infection process. To study the maturation pathway of the S glycoprotein of the severe acute respiratory syndrome (SARS)-coronavirus (CoV) within the host cell, a T7/vaccinia virus-based expression system coupled to immunoprecipitation with anti-S antibodies was used to test and analyze different forms of the S glycoprotein. The state of maturity of the S glycoprotein can be deduced from its sensitivity to hydrolysis by endoglycosidase H (EndoH) or N-glycosidase F (N-Gly F). A fully matured S glycoprotein will be modified with complex oligosaccharides which makes it resistant to cleavage by EndoH but not by N-Gly F. By exploiting this characteristic, it is then possible to determine which forms of the immunoprecipitated S protein are properly processed by the host cell. With this system, many different constructs of the S glycoprotein can be analyzed in parallel thus providing another method by which to study the functional domains of S involved in membrane fusion event that occurs during viral infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17502675</PMID><DateCompleted><Year>2007</Year><Month>06</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1064-3745</ISSN><JournalIssue CitedMedium="Print"><Volume>379</Volume><PubDate><Year>2007</Year></PubDate></JournalIssue><Title>Methods in molecular biology (Clifton, N.J.)</Title><ISOAbbreviation>Methods Mol. Biol.</ISOAbbreviation></Journal><ArticleTitle>Expression, glycosylation, and modification of the spike (S) glycoprotein of SARS CoV.</ArticleTitle><Pagination><MedlinePgn>127-35</MedlinePgn></Pagination><Abstract><AbstractText>The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. To study the maturation pathway of the S glycoprotein of the severe acute respiratory syndrome (SARS)-coronavirus (CoV) within the host cell, a T7/vaccinia virus-based expression system coupled to immunoprecipitation with anti-S antibodies was used to test and analyze different forms of the S glycoprotein. The state of maturity of the S glycoprotein can be deduced from its sensitivity to hydrolysis by endoglycosidase H (EndoH) or N-glycosidase F (N-Gly F). A fully matured S glycoprotein will be modified with complex oligosaccharides which makes it resistant to cleavage by EndoH but not by N-Gly F. By exploiting this characteristic, it is then possible to determine which forms of the immunoprecipitated S protein are properly processed by the host cell. With this system, many different constructs of the S glycoprotein can be analyzed in parallel thus providing another method by which to study the functional domains of S involved in membrane fusion event that occurs during viral infection.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shen</LastName><ForeName>Shuo</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Collaborative Antiviral Research Group, Institute of Molecular and Cell Biology, Proteos, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Timothy H P</ForeName><Initials>TH</Initials></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Yee-Joo</ForeName><Initials>YJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Methods Mol Biol</MedlineTA><NlmUniqueID>9214969</NlmUniqueID><ISSNLinking>1064-3745</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike 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UI="D017038" MajorTopicYN="N">Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D043524" MajorTopicYN="N">Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046188" MajorTopicYN="N">Protein Modification, Translational</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="Y">SARS Virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014616" MajorTopicYN="N">Vaccinia virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>7</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>5</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>6</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>5</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17502675</ArticleId><ArticleId IdType="pii">1-59745-393-5:127</ArticleId><ArticleId IdType="doi">10.1007/978-1-59745-393-6_9</ArticleId><ArticleId IdType="pmc">PMC7120769</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Lancet. 2003 May 24;361(9371):1779-85</Citation><ArticleIdList><ArticleId IdType="pubmed">12781537</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2006 Jan;80(2):941-50</Citation><ArticleIdList><ArticleId IdType="pubmed">16378996</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virology. 2004 Sep 1;326(2):288-98</Citation><ArticleIdList><ArticleId IdType="pubmed">15302214</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2005 Mar;79(6):3289-96</Citation><ArticleIdList><ArticleId IdType="pubmed">15731223</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 1994 Sep;68(9):5772-80</Citation><ArticleIdList><ArticleId IdType="pubmed">8057459</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Aug 30;102(35):12543-7</Citation><ArticleIdList><ArticleId IdType="pubmed">16116101</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Cell Biol. 1997 Nov 3;139(3):613-23</Citation><ArticleIdList><ArticleId IdType="pubmed">9348279</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Singapour</li></country></list><tree><noCountry><name sortKey="Tan, Timothy H P" sort="Tan, Timothy H P" uniqKey="Tan T" first="Timothy H P" last="Tan">Timothy H P. Tan</name><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name></noCountry><country name="Singapour"><noRegion><name sortKey="Shen, Shuo" sort="Shen, Shuo" uniqKey="Shen S" first="Shuo" last="Shen">Shuo Shen</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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