Folding of the mouse hepatitis virus spike protein and its association with the membrane protein.
Identifieur interne : 003418 ( PubMed/Checkpoint ); précédent : 003417; suivant : 003419Folding of the mouse hepatitis virus spike protein and its association with the membrane protein.
Auteurs : D J Opstelten [Pays-Bas] ; P. De Groote ; M C Horzinek ; P J RottierSource :
- Archives of virology. Supplementum [ 0939-1983 ] ; 1994.
Descripteurs français
- KwdFr :
- Disulfures, Dithiothréitol (pharmacologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (métabolisme), Oxydoréduction, Pliage des protéines, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme), Protéines de la matrice virale (métabolisme), Réplication virale, Transport biologique, Virus de l'hépatite murine (croissance et développement), Virus de l'hépatite murine (métabolisme).
- MESH :
- croissance et développement : Virus de l'hépatite murine.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines de la matrice virale, Virus de l'hépatite murine.
- pharmacologie : Dithiothréitol.
- Disulfures, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Oxydoréduction, Pliage des protéines, Protéines de l'enveloppe virale, Réplication virale, Transport biologique.
English descriptors
- KwdEn :
- Biological Transport, Disulfides, Dithiothreitol (pharmacology), Membrane Glycoproteins (drug effects), Membrane Glycoproteins (metabolism), Murine hepatitis virus (growth & development), Murine hepatitis virus (metabolism), Oxidation-Reduction, Protein Folding, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (drug effects), Viral Envelope Proteins (metabolism), Viral Matrix Proteins (metabolism), Virus Replication.
- MESH :
- chemical , drug effects : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins, Viral Matrix Proteins.
- chemical , pharmacology : Dithiothreitol.
- chemical : Disulfides, Spike Glycoprotein, Coronavirus.
- growth & development : Murine hepatitis virus.
- metabolism : Murine hepatitis virus.
- Biological Transport, Oxidation-Reduction, Protein Folding, Virus Replication.
Abstract
Coronaviruses are assembled by budding into pre-Golgi membranes. Using different approaches we have demonstrated that the spike (S) protein and the membrane (M) protein of mouse hepatitis virus (MHV) associate to form large complexes. Newly synthesized M was found in these complexes almost immediately after its synthesis, whereas the S protein started to appear in heterocomplexes after 10-20 min. This is consistent with the slow rate of folding of S and with the observation that folding of S preceeds its association with M. While the folding of S involves the formation of multiple disulfide bonds, folding of M is disulfide-independent. This contrast was reflected by the differential sensitivity of the two proteins to reduction with dithiothreitol (DTT). Addition of DTT to the culture medium of MHV-infected cells drastically impaired the folding of S, but not of M. Consequently, the S protein was unable to interact with M. Under these conditions, S stayed in the ER while M was transported efficiently beyond the site of budding to the Golgi complex. We conclude that the association of S with M is an essential step in the formation of the viral envelope and in the accumulation of both proteins at the site of virus assembly.
DOI: 10.1007/978-3-7091-9326-6_32
PubMed: 8032264
Affiliations:
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De Groote</name></author><author><name sortKey="Horzinek, M C" sort="Horzinek, M C" uniqKey="Horzinek M" first="M C" last="Horzinek">M C Horzinek</name></author><author><name sortKey="Rottier, P J" sort="Rottier, P J" uniqKey="Rottier P" first="P J" last="Rottier">P J Rottier</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:8032264</idno><idno type="pmid">8032264</idno><idno type="doi">10.1007/978-3-7091-9326-6_32</idno><idno type="wicri:Area/PubMed/Corpus">003532</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003532</idno><idno type="wicri:Area/PubMed/Curation">003532</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">003532</idno><idno type="wicri:Area/PubMed/Checkpoint">003418</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">003418</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Folding of the mouse hepatitis virus spike protein and its association with the membrane protein.</title><author><name sortKey="Opstelten, D J" sort="Opstelten, D J" uniqKey="Opstelten D" first="D J" last="Opstelten">D J Opstelten</name><affiliation wicri:level="4"><nlm:affiliation>Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University</wicri:regionArea><placeName><settlement type="city">Utrecht</settlement><region nuts="2">Utrecht (province)</region></placeName><orgName type="university">Université d'Utrecht</orgName></affiliation></author><author><name sortKey="De Groote, P" sort="De Groote, P" uniqKey="De Groote P" first="P" last="De Groote">P. De Groote</name></author><author><name sortKey="Horzinek, M C" sort="Horzinek, M C" uniqKey="Horzinek M" first="M C" last="Horzinek">M C Horzinek</name></author><author><name sortKey="Rottier, P J" sort="Rottier, P J" uniqKey="Rottier P" first="P J" last="Rottier">P J Rottier</name></author></analytic><series><title level="j">Archives of virology. 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Using different approaches we have demonstrated that the spike (S) protein and the membrane (M) protein of mouse hepatitis virus (MHV) associate to form large complexes. Newly synthesized M was found in these complexes almost immediately after its synthesis, whereas the S protein started to appear in heterocomplexes after 10-20 min. This is consistent with the slow rate of folding of S and with the observation that folding of S preceeds its association with M. While the folding of S involves the formation of multiple disulfide bonds, folding of M is disulfide-independent. This contrast was reflected by the differential sensitivity of the two proteins to reduction with dithiothreitol (DTT). Addition of DTT to the culture medium of MHV-infected cells drastically impaired the folding of S, but not of M. Consequently, the S protein was unable to interact with M. Under these conditions, S stayed in the ER while M was transported efficiently beyond the site of budding to the Golgi complex. We conclude that the association of S with M is an essential step in the formation of the viral envelope and in the accumulation of both proteins at the site of virus assembly.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8032264</PMID><DateCompleted><Year>1994</Year><Month>08</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0939-1983</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><PubDate><Year>1994</Year></PubDate></JournalIssue><Title>Archives of virology. Supplementum</Title><ISOAbbreviation>Arch. Virol. Suppl.</ISOAbbreviation></Journal><ArticleTitle>Folding of the mouse hepatitis virus spike protein and its association with the membrane protein.</ArticleTitle><Pagination><MedlinePgn>319-28</MedlinePgn></Pagination><Abstract><AbstractText>Coronaviruses are assembled by budding into pre-Golgi membranes. Using different approaches we have demonstrated that the spike (S) protein and the membrane (M) protein of mouse hepatitis virus (MHV) associate to form large complexes. Newly synthesized M was found in these complexes almost immediately after its synthesis, whereas the S protein started to appear in heterocomplexes after 10-20 min. This is consistent with the slow rate of folding of S and with the observation that folding of S preceeds its association with M. While the folding of S involves the formation of multiple disulfide bonds, folding of M is disulfide-independent. This contrast was reflected by the differential sensitivity of the two proteins to reduction with dithiothreitol (DTT). Addition of DTT to the culture medium of MHV-infected cells drastically impaired the folding of S, but not of M. Consequently, the S protein was unable to interact with M. Under these conditions, S stayed in the ER while M was transported efficiently beyond the site of budding to the Golgi complex. We conclude that the association of S with M is an essential step in the formation of the viral envelope and in the accumulation of both proteins at the site of virus assembly.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Opstelten</LastName><ForeName>D J</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Groote</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Horzinek</LastName><ForeName>M C</ForeName><Initials>MC</Initials></Author><Author ValidYN="Y"><LastName>Rottier</LastName><ForeName>P J</ForeName><Initials>PJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Austria</Country><MedlineTA>Arch Virol Suppl</MedlineTA><NlmUniqueID>9214275</NlmUniqueID><ISSNLinking>0939-1983</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><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="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014763">Viral Matrix 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IdType="doi">10.1007/978-3-7091-9326-6_32</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Pays-Bas</li></country><region><li>Utrecht (province)</li></region><settlement><li>Utrecht</li></settlement><orgName><li>Université d'Utrecht</li></orgName></list><tree><noCountry><name sortKey="De Groote, P" sort="De Groote, P" uniqKey="De Groote P" first="P" last="De Groote">P. De Groote</name><name sortKey="Horzinek, M C" sort="Horzinek, M C" uniqKey="Horzinek M" first="M C" last="Horzinek">M C Horzinek</name><name sortKey="Rottier, P J" sort="Rottier, P J" uniqKey="Rottier P" first="P J" last="Rottier">P J Rottier</name></noCountry><country name="Pays-Bas"><region name="Utrecht (province)"><name sortKey="Opstelten, D J" sort="Opstelten, D J" uniqKey="Opstelten D" first="D J" last="Opstelten">D J Opstelten</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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