Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M.
Identifieur interne : 002347 ( PubMed/Corpus ); précédent : 002346; suivant : 002348Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M.
Auteurs : M. Oostra ; C A M. De Haan ; R J De Groot ; P J M. RottierSource :
- Journal of virology [ 0022-538X ] ; 2006.
English descriptors
- KwdEn :
- Amino Acid Sequence, Gene Expression, Glycosylation, Molecular Sequence Data, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (metabolism), Protein Modification, Translational, Protein Processing, Post-Translational, Radioisotopes, SARS Virus (chemistry), Sialic Acids (analysis), Staining and Labeling, Viral Matrix Proteins (chemistry), Viral Matrix Proteins (metabolism), Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , analysis : Sialic Acids.
- chemical , chemistry : Viral Matrix Proteins, Viral Proteins.
- chemical , metabolism : Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Viral Matrix Proteins, Viral Proteins.
- chemistry : SARS Virus.
- Amino Acid Sequence, Gene Expression, Glycosylation, Molecular Sequence Data, Protein Modification, Translational, Protein Processing, Post-Translational, Radioisotopes, Staining and Labeling.
Abstract
The severe acute respiratory syndrome coronavirus (SARS-CoV) open reading frame 3a protein has recently been shown to be a structural protein. The protein is encoded by one of the so-called group-specific genes and has no sequence homology with any of the known structural or group-specific proteins of coronaviruses. It does, however, have several similarities to the coronavirus M proteins; (i) they are triple membrane spanning with the same topology, (ii) they have similar intracellular localizations (predominantly Golgi), (iii) both are viral structural proteins, and (iv) they appear to interact with the E and S proteins, as well as with each other. The M protein plays a crucial role in coronavirus assembly and is glycosylated in all coronaviruses, either by N-linked or by O-linked oligosaccharides. The conserved glycosylation of the coronavirus M proteins and the resemblance of the 3a protein to them led us to investigate the glycosylation of these two SARS-CoV membrane proteins. The proteins were expressed separately using the vaccinia virus T7 expression system, followed by metabolic labeling. Pulse-chase analysis showed that both proteins were modified, although in different ways. While the M protein acquired cotranslationally oligosaccharides that could be removed by PNGaseF, the 3a protein acquired its modifications posttranslationally, and they were not sensitive to the N-glycosidase enzyme. The SARS-CoV 3a protein, however, was demonstrated to contain sialic acids, indicating the presence of oligosaccharides. O-glycosylation of the 3a protein was indeed confirmed using an in situ O-glycosylation assay of endoplasmic reticulum-retained mutants. In addition, we showed that substitution of serine and threonine residues in the ectodomain of the 3a protein abolished the addition of the O-linked sugars. Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.
DOI: 10.1128/JVI.80.5.2326-2336.2006
PubMed: 16474139
Links to Exploration step
pubmed:16474139Le document en format XML
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Rottier</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16474139</idno><idno type="pmid">16474139</idno><idno type="doi">10.1128/JVI.80.5.2326-2336.2006</idno><idno type="wicri:Area/PubMed/Corpus">002347</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002347</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M.</title><author><name sortKey="Oostra, M" sort="Oostra, M" uniqKey="Oostra M" first="M" last="Oostra">M. Oostra</name><affiliation><nlm:affiliation>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, The Netherlands.</nlm:affiliation></affiliation></author><author><name sortKey="De Haan, C A M" sort="De Haan, C A M" uniqKey="De Haan C" first="C A M" last="De Haan">C A M. De Haan</name></author><author><name sortKey="De Groot, R J" sort="De Groot, R J" uniqKey="De Groot R" first="R J" last="De Groot">R J De Groot</name></author><author><name sortKey="Rottier, P J M" sort="Rottier, P J M" uniqKey="Rottier P" first="P J M" last="Rottier">P J M. Rottier</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Gene Expression</term><term>Glycosylation</term><term>Molecular Sequence Data</term><term>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (metabolism)</term><term>Protein Modification, Translational</term><term>Protein Processing, Post-Translational</term><term>Radioisotopes</term><term>SARS Virus (chemistry)</term><term>Sialic Acids (analysis)</term><term>Staining and Labeling</term><term>Viral Matrix Proteins (chemistry)</term><term>Viral Matrix Proteins (metabolism)</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Sialic Acids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Matrix Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase</term><term>Viral Matrix Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Gene Expression</term><term>Glycosylation</term><term>Molecular Sequence Data</term><term>Protein Modification, Translational</term><term>Protein Processing, Post-Translational</term><term>Radioisotopes</term><term>Staining and Labeling</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) open reading frame 3a protein has recently been shown to be a structural protein. The protein is encoded by one of the so-called group-specific genes and has no sequence homology with any of the known structural or group-specific proteins of coronaviruses. It does, however, have several similarities to the coronavirus M proteins; (i) they are triple membrane spanning with the same topology, (ii) they have similar intracellular localizations (predominantly Golgi), (iii) both are viral structural proteins, and (iv) they appear to interact with the E and S proteins, as well as with each other. The M protein plays a crucial role in coronavirus assembly and is glycosylated in all coronaviruses, either by N-linked or by O-linked oligosaccharides. The conserved glycosylation of the coronavirus M proteins and the resemblance of the 3a protein to them led us to investigate the glycosylation of these two SARS-CoV membrane proteins. The proteins were expressed separately using the vaccinia virus T7 expression system, followed by metabolic labeling. Pulse-chase analysis showed that both proteins were modified, although in different ways. While the M protein acquired cotranslationally oligosaccharides that could be removed by PNGaseF, the 3a protein acquired its modifications posttranslationally, and they were not sensitive to the N-glycosidase enzyme. The SARS-CoV 3a protein, however, was demonstrated to contain sialic acids, indicating the presence of oligosaccharides. O-glycosylation of the 3a protein was indeed confirmed using an in situ O-glycosylation assay of endoplasmic reticulum-retained mutants. In addition, we showed that substitution of serine and threonine residues in the ectodomain of the 3a protein abolished the addition of the O-linked sugars. Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16474139</PMID><DateCompleted><Year>2006</Year><Month>03</Month><Day>17</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>80</Volume><Issue>5</Issue><PubDate><Year>2006</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M.</ArticleTitle><Pagination><MedlinePgn>2326-36</MedlinePgn></Pagination><Abstract><AbstractText>The severe acute respiratory syndrome coronavirus (SARS-CoV) open reading frame 3a protein has recently been shown to be a structural protein. The protein is encoded by one of the so-called group-specific genes and has no sequence homology with any of the known structural or group-specific proteins of coronaviruses. It does, however, have several similarities to the coronavirus M proteins; (i) they are triple membrane spanning with the same topology, (ii) they have similar intracellular localizations (predominantly Golgi), (iii) both are viral structural proteins, and (iv) they appear to interact with the E and S proteins, as well as with each other. The M protein plays a crucial role in coronavirus assembly and is glycosylated in all coronaviruses, either by N-linked or by O-linked oligosaccharides. The conserved glycosylation of the coronavirus M proteins and the resemblance of the 3a protein to them led us to investigate the glycosylation of these two SARS-CoV membrane proteins. The proteins were expressed separately using the vaccinia virus T7 expression system, followed by metabolic labeling. Pulse-chase analysis showed that both proteins were modified, although in different ways. While the M protein acquired cotranslationally oligosaccharides that could be removed by PNGaseF, the 3a protein acquired its modifications posttranslationally, and they were not sensitive to the N-glycosidase enzyme. The SARS-CoV 3a protein, however, was demonstrated to contain sialic acids, indicating the presence of oligosaccharides. O-glycosylation of the 3a protein was indeed confirmed using an in situ O-glycosylation assay of endoplasmic reticulum-retained mutants. In addition, we showed that substitution of serine and threonine residues in the ectodomain of the 3a protein abolished the addition of the O-linked sugars. Thus, the SARS-CoV 3a protein is an O-glycosylated glycoprotein, like the group 2 coronavirus M proteins but unlike the SARS-CoV M protein, which is N glycosylated.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Oostra</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Haan</LastName><ForeName>C A M</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>de Groot</LastName><ForeName>R J</ForeName><Initials>RJ</Initials></Author><Author ValidYN="Y"><LastName>Rottier</LastName><ForeName>P J M</ForeName><Initials>PJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United 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