About: Tunicamycin resistant glycosylation of a coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein

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About: Tunicamycin resistant glycosylation of a coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Tunicamycin resistant glycosylation of a coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein
Creator	Holmes, Kathryn Doller, Elizabeth Sturmant, Lawrence
Source	Elsevier; Medline; PMC
abstract	Abstract Tunicamycin has different effects on the glycosylation of the two envelope glycoproteins of mouse hepatitis virus (MHV), a coronavirus. Unlike envelope glycoproteins of other viruses, the transmembrane glycoprotein El is glycosylated normally in the presence of tunicamycin. This suggests that glycosylation of El does not involve transfer of core oligosaccharides from dolichol pyrophosphate intermediates to asparagine residues, but may occur by 0-linked glycosylation of serine or threonine residues. Synthesis of the peplomeric glycoprotein E2 is not readily detectable in the presence of tunicamycin. Inhibition of N-linked glycosylation of E2 by tunicamycin either prevents synthesis or facilitates degradation of the protein moiety of E2. Radiolabeling with carbohydrate precursors and borate gel electrophoresis of glycopeptides show that different oligcsaccharide side chains are attached to El and E2. The two coronavirus envelope glycoproteins thus appear to be glycosylated by different mechanisms. In tunicamycin-treated cells, noninfectious virions lacking peplomers are formed at intracytoplasmic membranes and released from the cells. These virions contain normal amounts of nucleocapsid protein and glycosylated El, but lack E2. Thus the transmembrane glycoprotein El is the only viral glycoprotein required for the formation of the viral envelope or for virus maturation and release. The peplomeric glycoprotein E2 appears to be required for attachment to virus receptors on the plasma membrane. The coronavirus envelope envelope glycoprotein E1 appears to be a novel type of viral glycoprotein which is post-translationally glycosylated by a tunicamycin-resistant process that yields oligosaccharide side chains different from those of N-linked glycoproteins. These findings suggest that El may be particularly useful as a model for studying the biosynthesis, glycosylation, and intracellular transport of 0-linked glycoproteins.
has issue date	1981-12-31(xsd:dateTime)
bibo:doi	10.1016/0042-6822(81)90115-x
bibo:pmid	7314449
has license	els-covid
sha1sum (hex)	d5178260b84dc4639c9287f916e3709c84a0ff39
schema:url	https://doi.org/10.1016/0042-6822%2881%2990115-x
resource representing a document's title	Tunicamycin resistant glycosylation of a coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein
has PubMed Central identifier	PMC7130623
has PubMed identifier	7314449
schema:publication	Virology
resource representing a document's body	covid:d5178260b84dc4639c9287f916e3709c84a0ff39#body_text
is schema:about of	named entity 'NOVEL' named entity 'dolichol' named entity 'residues' named entity 'threonine' named entity 'presence' named entity 'Synthesis' named entity 'N-linked glycosylation' named entity 'facilitates' named entity 'O-linked glycosylation' named entity 'These' named entity 'O-linked' named entity 'viral envelope' named entity 'carbohydrate' named entity 'MHV' named entity 'glycoprotein' named entity 'virus' named entity 'GLYCOPEPTIDES' named entity 'OCCUR' named entity 'RADIOLABELING' named entity 'NORMAL' named entity 'O-LINKED GLYCOPROTEINS' named entity 'ATTACHMENT' named entity 'LACKING' named entity 'VIRAL GLYCOPROTEIN' named entity 'VIRUS RECEPTORS' named entity 'OLIGOSACCHARIDES' named entity 'CARBOHYDRATE' named entity 'INHIBITION' named entity 'MOUSE HEPATITIS VIRUS' named entity 'MECHANISMS' named entity 'MAY BE' named entity 'TRANSMEMBRANE GLYCOPROTEIN' named entity 'PROTEIN ' named entity 'TREATED' named entity 'NOVEL' named entity 'BUT' named entity 'ENVELOPE GLYCOPROTEIN' named entity 'DETECTABLE' named entity 'LACK' named entity 'FORMED' named entity 'N-LINKED GLYCOSYLATION' named entity 'AMOUNTS' named entity 'DOLICHOL PYROPHOSPHATE' named entity 'TYPE' named entity 'EITHER' named entity 'ASPARAGINE' named entity 'INTRACELLULAR TRANSPORT' named entity 'CONTAIN' named entity 'PRESENCE OF' named entity 'PLASMA MEMBRANE' named entity 'APPEAR' named entity 'GLYCOPROTEIN' named entity 'CORONAVIRUS' named entity 'SERINE' named entity 'DIFFERENT' named entity 'GLYCOSYLATED' named entity 'DOES NOT' named entity 'GEL ELECTROPHORESIS' named entity 'FORMATION' named entity 'PREVENTS' named entity 'USEFUL' named entity 'VIRUSES' named entity 'BORATE' named entity 'NONINFECTIOUS' named entity 'THREONINE' named entity 'REQUIRED' named entity 'SYNTHESIS' named entity 'GLYCOPROTEINS' named entity 'RESISTANT' named entity 'SUGGEST' named entity 'RELEASED' named entity 'VIRUS MATURATION' named entity 'DEMONSTRATION' named entity 'RELEASE' named entity 'VIRAL GLYCOPROTEIN' named entity 'TYPE' named entity 'THESE' named entity 'BIOSYNTHESIS' named entity 'CELLS'

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