| pubmed-article:17761532 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17761532 | lifeskim:mentions | umls-concept:C2700280 | lld:lifeskim |
| pubmed-article:17761532 | lifeskim:mentions | umls-concept:C1819995 | lld:lifeskim |
| pubmed-article:17761532 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:17761532 | lifeskim:mentions | umls-concept:C0205671 | lld:lifeskim |
| pubmed-article:17761532 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:17761532 | lifeskim:mentions | umls-concept:C1312042 | lld:lifeskim |
| pubmed-article:17761532 | lifeskim:mentions | umls-concept:C0580836 | lld:lifeskim |
| pubmed-article:17761532 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:17761532 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:17761532 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:17761532 | pubmed:dateCreated | 2007-10-26 | lld:pubmed |
| pubmed-article:17761532 | pubmed:abstractText | alpha-Dystroglycan (alpha-DG) is an important cellular receptor for extracellular matrix (ECM) proteins as well as the Old World arenaviruses lymphocytic choriomeningitis virus (LCMV) and the human pathogenic Lassa fever virus (LFV). Specific O-glycosylation of alpha-DG is critical for its function as receptor for ECM proteins and arenaviruses. Here, we investigated the impact of arenavirus infection on alpha-DG expression. Infection with an immunosuppressive LCMV isolate caused a marked reduction in expression of functional alpha-DG without affecting biosynthesis of DG core protein or global cell surface glycoprotein expression. The effect was caused by the viral glycoprotein (GP), and it critically depended on alpha-DG binding affinity and GP maturation. An equivalent effect was observed with LFVGP. Viral GP was found to associate with a complex between DG and the glycosyltransferase LARGE in the Golgi. Overexpression of LARGE restored functional alpha-DG expression in infected cells. We provide evidence that virus-induced down-modulation of functional alpha-DG perturbs DG-mediated assembly of laminin at the cell surface, affecting normal cell-matrix interactions. | lld:pubmed |
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| pubmed-article:17761532 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17761532 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17761532 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17761532 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17761532 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:17761532 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:17761532 | pubmed:author | pubmed-author:CampbellKevin... | lld:pubmed |
| pubmed-article:17761532 | pubmed:author | pubmed-author:OldstoneMicha... | lld:pubmed |
| pubmed-article:17761532 | pubmed:author | pubmed-author:KunzStefanS | lld:pubmed |
| pubmed-article:17761532 | pubmed:author | pubmed-author:RojekJillian... | lld:pubmed |
| pubmed-article:17761532 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17761532 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:17761532 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17761532 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17761532 | pubmed:pagination | 4493-507 | lld:pubmed |
| pubmed-article:17761532 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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