Spike protein assembly into the coronavirion: exploring the limits of its sequence requirements.
Identifieur interne : 000E48 ( Ncbi/Merge ); précédent : 000E47; suivant : 000E49Spike protein assembly into the coronavirion: exploring the limits of its sequence requirements.
Auteurs : Berend Jan Bosch [Pays-Bas] ; Cornelis A M. De Haan ; Saskia L. Smits ; Peter J M. RottierSource :
- Virology [ 0042-6822 ] ; 2005.
Descripteurs français
- KwdFr :
- ARN viral (génétique), Animaux, Assemblage viral, Chats, Coronavirus félin (génétique), Coronavirus félin (métabolisme), Données de séquences moléculaires, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Humains, Lignée cellulaire, Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines de la matrice virale (génétique), Protéines de la matrice virale (métabolisme), Recombinaison génétique, Régulation de l'expression des gènes viraux, Souris, Séquence d'acides aminés, Séquence nucléotidique, Virion (métabolisme), Virus de l'hépatite murine (génétique), Virus de l'hépatite murine (métabolisme).
- MESH :
- génétique : ARN viral, Coronavirus félin, Glycoprotéines membranaires, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Protéines de la matrice virale, Virus de l'hépatite murine.
- métabolisme : Coronavirus félin, Glycoprotéines membranaires, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Protéines de la matrice virale, Virion, Virus de l'hépatite murine.
- Animaux, Assemblage viral, Chats, Données de séquences moléculaires, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Lignée cellulaire, Protéines de l'enveloppe virale, Recombinaison génétique, Régulation de l'expression des gènes viraux, Souris, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Base Sequence, Cats, Cell Line, Coronavirus, Feline (genetics), Coronavirus, Feline (metabolism), Gene Expression Regulation, Viral, Humans, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mice, Molecular Sequence Data, Murine hepatitis virus (genetics), Murine hepatitis virus (metabolism), RNA, Viral (genetics), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Recombination, Genetic, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism), Virion (metabolism), Virus Assembly.
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : Coronavirus, Feline, Membrane Glycoproteins, Murine hepatitis virus, RNA, Viral, Recombinant Fusion Proteins, Viral Envelope Proteins, Viral Matrix Proteins.
- metabolism : Coronavirus, Feline, Membrane Glycoproteins, Murine hepatitis virus, Recombinant Fusion Proteins, Viral Envelope Proteins, Viral Matrix Proteins, Virion.
- Amino Acid Sequence, Animals, Base Sequence, Cats, Cell Line, Gene Expression Regulation, Viral, Humans, Membrane Fusion, Mice, Molecular Sequence Data, Recombination, Genetic, Spike Glycoprotein, Coronavirus, Virus Assembly.
Abstract
The coronavirus spike (S) protein, required for receptor binding and membrane fusion, is incorporated into the assembling virion by interactions with the viral membrane (M) protein. Earlier we showed that the ectodomain of the S protein is not involved in this process. Here we further defined the requirements of the S protein for virion incorporation. We show that the cytoplasmic domain, not the transmembrane domain, determines the association with the M protein and suffices to effect the incorporation into viral particles of chimeric spikes as well as of foreign viral glycoproteins. The essential sequence was mapped to the membrane-proximal region of the cytoplasmic domain, which is also known to be of critical importance for the fusion function of the S protein. Consistently, only short C-terminal truncations of the S protein were tolerated when introduced into the virus by targeted recombination. The important role of the about 38-residues cytoplasmic domain in the assembly of and membrane fusion by this approximately 1300 amino acids long protein is discussed.
DOI: 10.1016/j.virol.2005.02.001
PubMed: 15780881
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002833
- to stream PubMed, to step Curation: 002833
- to stream PubMed, to step Checkpoint: 002470
Links to Exploration step
pubmed:15780881Le document en format XML
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gènes viraux</term><term>Souris</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The coronavirus spike (S) protein, required for receptor binding and membrane fusion, is incorporated into the assembling virion by interactions with the viral membrane (M) protein. Earlier we showed that the ectodomain of the S protein is not involved in this process. Here we further defined the requirements of the S protein for virion incorporation. We show that the cytoplasmic domain, not the transmembrane domain, determines the association with the M protein and suffices to effect the incorporation into viral particles of chimeric spikes as well as of foreign viral glycoproteins. The essential sequence was mapped to the membrane-proximal region of the cytoplasmic domain, which is also known to be of critical importance for the fusion function of the S protein. Consistently, only short C-terminal truncations of the S protein were tolerated when introduced into the virus by targeted recombination. The important role of the about 38-residues cytoplasmic domain in the assembly of and membrane fusion by this approximately 1300 amino acids long protein is discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15780881</PMID><DateCompleted><Year>2005</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">0042-6822</ISSN><JournalIssue CitedMedium="Print"><Volume>334</Volume><Issue>2</Issue><PubDate><Year>2005</Year><Month>Apr</Month><Day>10</Day></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>Spike protein assembly into the coronavirion: exploring the limits of its sequence requirements.</ArticleTitle><Pagination><MedlinePgn>306-18</MedlinePgn></Pagination><Abstract><AbstractText>The coronavirus spike (S) protein, required for receptor binding and membrane fusion, is incorporated into the assembling virion by interactions with the viral membrane (M) protein. Earlier we showed that the ectodomain of the S protein is not involved in this process. Here we further defined the requirements of the S protein for virion incorporation. We show that the cytoplasmic domain, not the transmembrane domain, determines the association with the M protein and suffices to effect the incorporation into viral particles of chimeric spikes as well as of foreign viral glycoproteins. The essential sequence was mapped to the membrane-proximal region of the cytoplasmic domain, which is also known to be of critical importance for the fusion function of the S protein. Consistently, only short C-terminal truncations of the S protein were tolerated when introduced into the virus by targeted recombination. The important role of the about 38-residues cytoplasmic domain in the assembly of and membrane fusion by this approximately 1300 amino acids long protein is discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bosch</LastName><ForeName>Berend Jan</ForeName><Initials>BJ</Initials><AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Haan</LastName><ForeName>Cornelis A M</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Smits</LastName><ForeName>Saskia L</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Rottier</LastName><ForeName>Peter J M</ForeName><Initials>PJ</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>United States</Country><MedlineTA>Virology</MedlineTA><NlmUniqueID>0110674</NlmUniqueID><ISSNLinking>0042-6822</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="D012367">RNA, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion 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="D014763">Viral Matrix Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical><Chemical><RegistryNumber>108502-71-2</RegistryNumber><NameOfSubstance UI="C067997">M protein, Coronavirus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002415" MajorTopicYN="N">Cats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016765" MajorTopicYN="N">Coronavirus, Feline</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015967" MajorTopicYN="N">Gene Expression Regulation, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008561" MajorTopicYN="N">Membrane Fusion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></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="D012367" MajorTopicYN="N">RNA, Viral</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011995" MajorTopicYN="N">Recombination, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><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></MeshHeading><MeshHeading><DescriptorName UI="D014771" MajorTopicYN="N">Virion</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019065" MajorTopicYN="Y">Virus Assembly</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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