Linked Life Data

2838571

Source:http://linkedlifedata.com/resource/pubmed/id/2838571

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1988-8-2
pubmed:abstractText
Three distinct families of glycoprotein complexes present in the envelopes of human cytomegalovirus and designated gcI, gcII and gcIII have been described recently. The synthesis of the gcI family was analysed using either inhibitors of glycoprotein processing and transport or endoglycosidase treatments of purified glycoproteins. The initial step in gcI synthesis involved the glycosylation of a 95K protein (p95) to form a high-mannose, simple N-linked glycoprotein of Mr 158K (gp158), which was detected only in the presence of the glycoprotein processing inhibitor castanospermine. This intermediate was rapidly trimmed in the virus-infected cell to form a more stable simple N-linked precursor glycoprotein of Mr 138K (gp138). Treatment of either gp158 or gp138 with endoglycosidase H produced p95. Both molecules, gp158 and gp138, were found in disulphide-linked complexes which are presumably infected cell precursors to gcI since they were not found in virions. The processing of these complexes involved complete cleavage of gp138 and conversion of some but not all of its oligosaccharide to complex N-linked chains. Both processing events were inhibited by the ionophore monensin. Mature gcI contained the gp138 cleavage product, gp93-130. The latter glycoprotein could be separated into two electrophoretic forms, gp93 and gp130. The deglycosylated form of gp55 had a discrete banding pattern with an apparent Mr of 46K (p46). In contrast, the deglycosylated forms of gp93 and gp130 had diffuse banding patterns with apparent Mr values of 46K to 56K (p46-56) and 60K to 70K (p60-70) respectively. Peptide profiles comparing gp93 with gp130 indicated that they have highly similar polypeptide backbones. Since the deglycosylated forms of gp55 and gp130, 46K and 60K to 70K, respectively, together exceed the 95K precursor/deglycosylated intermediate in Mr, we propose that the above glycoproteins are derived by an alternative proteolytic cleavage of the precursor. The heterogeneous electrophoretic properties of the deglycosylated forms of gp93 and gp130 may be due to additional post-translational modifications other than glycosylation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
69 ( Pt 6)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1205-15
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:2838571-Acetylglucosaminidase, pubmed-meshheading:2838571-Alkaloids, pubmed-meshheading:2838571-Autoradiography, pubmed-meshheading:2838571-Cells, Cultured, pubmed-meshheading:2838571-Cytomegalovirus, pubmed-meshheading:2838571-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:2838571-Glycoproteins, pubmed-meshheading:2838571-Glycoside Hydrolases, pubmed-meshheading:2838571-Glycosylation, pubmed-meshheading:2838571-Humans, pubmed-meshheading:2838571-Immunoassay, pubmed-meshheading:2838571-Indolizines, pubmed-meshheading:2838571-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, pubmed-meshheading:2838571-Monensin, pubmed-meshheading:2838571-Peptide Mapping, pubmed-meshheading:2838571-Protein Precursors, pubmed-meshheading:2838571-Protein Processing, Post-Translational, pubmed-meshheading:2838571-Swainsonine, pubmed-meshheading:2838571-Tunicamycin
pubmed:year
1988
pubmed:articleTitle
Characterization of a human cytomegalovirus glycoprotein complex (gcI).
pubmed:affiliation
Department of Microbiology, University of Iowa, Iowa City 52242.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't