Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3-4
|
| pubmed:dateCreated |
1993-3-17
|
| pubmed:abstractText |
In herpes simplex virus-infected (HSV) cells, the antiviral nucleoside analogue 5-n-propyl-2'-deoxyuridine (PdU) may, under certain circumstances, induce a pattern of interference with late steps in formation of N-linked glycans, resulting in increased availability of viral glycoproteins for neutralizing antibodies. The PdU-induced changes in N-linked glycans, released by pronase digestion of the HSV-specified glycoprotein gC-1, were investigated by using lectin affinity chromatography and Bio-Gel P6 gel filtration of glycans, radiolabelled with [3H]galactose or [3H]glucosamine. PdU-treatment of HSV-infected cells totally inhibited addition of sialic acid and reduced the amount of galactose incorporated into N-linked glycans by 70%. In addition, the PDU-treatment caused a decrease in oligosaccharides with affinity for Phaseoulus vulgaris leuco-agglutinin and erythro-agglutinin, and an increase in Lens culinaris lectin (LCA)-binding oligosaccharides, suggesting a PdU-induced shift from multi-branched to moderately branched structures. This shift was also found in HSV-infected B16 mouse melanoma cells, where the large content of multi-branched oligosaccharides contributes to the metastatic potential. The LCA-binding glycans from PdU-treated cells were smaller and contained less galactose units than corresponding structures from untreated cells. In a cell-free system, PdU 5'-monophosphate inhibited the translocation of UDP-GlcNAc, and, to a smaller extent, also the translocation of UDP-galactose into Golgi vesicles, suggesting that nucleotide sugar translocation is one important target for the PdU-induced interference with glycosylation in HSV-infected cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/5-propyl-2'-deoxyuridine,
http://linkedlifedata.com/resource/pubmed/chemical/Agglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/Antiviral Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Bromodeoxyuridine,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyuridine,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside Diphosphate Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/brivudine,
http://linkedlifedata.com/resource/pubmed/chemical/glycoprotein gC, herpes simplex...
|
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0304-8608
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
128
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
241-56
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8382038-Agglutinins,
pubmed-meshheading:8382038-Animals,
pubmed-meshheading:8382038-Antiviral Agents,
pubmed-meshheading:8382038-Biological Transport,
pubmed-meshheading:8382038-Bromodeoxyuridine,
pubmed-meshheading:8382038-Cell Line,
pubmed-meshheading:8382038-Cercopithecus aethiops,
pubmed-meshheading:8382038-Chromatography, Affinity,
pubmed-meshheading:8382038-Chromatography, Gel,
pubmed-meshheading:8382038-Deoxyuridine,
pubmed-meshheading:8382038-Glycosylation,
pubmed-meshheading:8382038-Golgi Apparatus,
pubmed-meshheading:8382038-Humans,
pubmed-meshheading:8382038-Infant,
pubmed-meshheading:8382038-Lectins,
pubmed-meshheading:8382038-Melanoma, Experimental,
pubmed-meshheading:8382038-Mice,
pubmed-meshheading:8382038-Neuraminidase,
pubmed-meshheading:8382038-Nucleoside Diphosphate Sugars,
pubmed-meshheading:8382038-Polysaccharides,
pubmed-meshheading:8382038-Simplexvirus,
pubmed-meshheading:8382038-Tumor Cells, Cultured,
pubmed-meshheading:8382038-Viral Envelope Proteins
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
5-Propyl-2-deoxyuridine induced interference with glycosylation in herpes simplex virus infected cells. Nature of PdU-induced modifications of N-linked glycans.
|
| pubmed:affiliation |
Department of Clinical Virology, University of Göteborg, Sweden.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|