Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity.
Identifieur interne : 003541 ( PubMed/Curation ); précédent : 003540; suivant : 003542Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity.
Auteurs : R. Stauber [Allemagne] ; M. Pfleiderera ; S. SiddellSource :
- The Journal of general virology [ 0022-1317 ] ; 1993.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Glycoprotéines membranaires (physiologie), Protéines de fusion virale (métabolisme), Protéines de l'enveloppe virale, Protéines de la matrice virale (génétique), Protéines de la matrice virale (métabolisme), Protéines de la matrice virale (physiologie), Séquence d'acides aminés, Séquence nucléotidique, Virus de l'hépatite murine (génétique), Virus de l'hépatite murine (métabolisme).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de la matrice virale, Virus de l'hépatite murine.
- métabolisme : Glycoprotéines membranaires, Protéines de fusion virale, Protéines de la matrice virale, Virus de l'hépatite murine.
- physiologie : Glycoprotéines membranaires, Protéines de la matrice virale.
- Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Protéines de l'enveloppe virale, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Base Sequence, Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Membrane Glycoproteins (physiology), Molecular Sequence Data, Murine hepatitis virus (genetics), Murine hepatitis virus (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins, Viral Fusion Proteins (metabolism), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism), Viral Matrix Proteins (physiology).
- MESH :
- chemical , genetics : Membrane Glycoproteins, Viral Matrix Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Fusion Proteins, Viral Matrix Proteins.
- chemical , physiology : Membrane Glycoproteins, Viral Matrix Proteins.
- genetics : Murine hepatitis virus.
- metabolism : Murine hepatitis virus.
- Amino Acid Sequence, Base Sequence, Molecular Sequence Data, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins.
Abstract
A cDNA copy of the murine coronavirus [otherwise known as murine hepatitis virus (MHV)] surface (S) glycoprotein gene was isolated and expressed in DBT cells by using a recombinant vaccinia virus system. The expressed S protein induced extensive syncytium formation at neutral pH. Oligonucleotide mutagenesis was used to engineer an S protein gene in which codons for the proteolytic cleavage site, Arg-Arg-Ala-Arg-Arg, were replaced with an equal number of codons for amino acids with aliphatic or aliphatic hydroxyl side-chains. The mutated S protein was stably expressed in DBT cells and, in contrast to the wild-type protein, was not proteolytically cleaved. Nevertheless, the non-cleaved protein induced extensive syncytium formation. These results clearly indicate that the non-cleaved form of the MHV S protein is able to mediate cell membrane fusion. Thus proteolytic cleavage is not an absolute requirement for fusion activity.
DOI: 10.1099/0022-1317-74-2-183
PubMed: 8381459
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pubmed:8381459Le document en format XML
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The expressed S protein induced extensive syncytium formation at neutral pH. Oligonucleotide mutagenesis was used to engineer an S protein gene in which codons for the proteolytic cleavage site, Arg-Arg-Ala-Arg-Arg, were replaced with an equal number of codons for amino acids with aliphatic or aliphatic hydroxyl side-chains. The mutated S protein was stably expressed in DBT cells and, in contrast to the wild-type protein, was not proteolytically cleaved. Nevertheless, the non-cleaved protein induced extensive syncytium formation. These results clearly indicate that the non-cleaved form of the MHV S protein is able to mediate cell membrane fusion. Thus proteolytic cleavage is not an absolute requirement for fusion activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8381459</PMID><DateCompleted><Year>1993</Year><Month>03</Month><Day>08</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-1317</ISSN><JournalIssue CitedMedium="Print"><Volume>74 ( Pt 2)</Volume><PubDate><Year>1993</Year><Month>Feb</Month></PubDate></JournalIssue><Title>The Journal of general virology</Title><ISOAbbreviation>J. Gen. Virol.</ISOAbbreviation></Journal><ArticleTitle>Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity.</ArticleTitle><Pagination><MedlinePgn>183-91</MedlinePgn></Pagination><Abstract><AbstractText>A cDNA copy of the murine coronavirus [otherwise known as murine hepatitis virus (MHV)] surface (S) glycoprotein gene was isolated and expressed in DBT cells by using a recombinant vaccinia virus system. The expressed S protein induced extensive syncytium formation at neutral pH. Oligonucleotide mutagenesis was used to engineer an S protein gene in which codons for the proteolytic cleavage site, Arg-Arg-Ala-Arg-Arg, were replaced with an equal number of codons for amino acids with aliphatic or aliphatic hydroxyl side-chains. The mutated S protein was stably expressed in DBT cells and, in contrast to the wild-type protein, was not proteolytically cleaved. Nevertheless, the non-cleaved protein induced extensive syncytium formation. These results clearly indicate that the non-cleaved form of the MHV S protein is able to mediate cell membrane fusion. Thus proteolytic cleavage is not an absolute requirement for fusion activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stauber</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Institute of Virology, University of Würzburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pfleiderera</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Siddell</LastName><ForeName>S</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Gen Virol</MedlineTA><NlmUniqueID>0077340</NlmUniqueID><ISSNLinking>0022-1317</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="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014760">Viral Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014763">Viral Matrix Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006517" MajorTopicYN="N">Murine hepatitis virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="Y">Viral Envelope Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014760" MajorTopicYN="N">Viral Fusion Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014763" MajorTopicYN="N">Viral Matrix Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1993</Year><Month>2</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1993</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1993</Year><Month>2</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8381459</ArticleId><ArticleId IdType="doi">10.1099/0022-1317-74-2-183</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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