Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M.
Identifieur interne : 001375 ( Ncbi/Checkpoint ); précédent : 001374; suivant : 001376Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M.
Auteurs : M. Oostra [Pays-Bas] ; C A M. De Haan ; R J De Groot ; P J M. RottierSource :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- KwdFr :
- Acides sialiques (analyse), Coloration et marquage, Données de séquences moléculaires, Expression des gènes, Glycosylation, Maturation post-traductionnelle des protéines, Modification traductionnelle des protéines, Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (métabolisme), Protéines de la matrice virale (), Protéines de la matrice virale (métabolisme), Protéines virales (), Protéines virales (métabolisme), Radio-isotopes, Séquence d'acides aminés, Virus du SRAS ().
- MESH :
- analyse : Acides sialiques.
- métabolisme : Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase, Protéines de la matrice virale, Protéines virales.
- Coloration et marquage, Données de séquences moléculaires, Expression des gènes, Glycosylation, Maturation post-traductionnelle des protéines, Modification traductionnelle des protéines, Protéines de la matrice virale, Protéines virales, Radio-isotopes, Séquence d'acides aminés, Virus du SRAS.
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
Affiliations:
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pubmed:16474139Le document en format XML
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<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>
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<term>Maturation post-traductionnelle des protéines</term>
<term>Modification traductionnelle des protéines</term>
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<term>Radio-isotopes</term>
<term>Séquence d'acides aminés</term>
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<term>Protéines de la matrice virale</term>
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<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>
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