Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1203275#aggregation> ?p ?o. }
Showing items 1 to 37 of
37
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B435686.
- aggregation creator B435687.
- aggregation creator B435688.
- aggregation creator B435689.
- aggregation creator B435690.
- aggregation creator person.
- aggregation date "2005".
- aggregation format "application/pdf".
- aggregation hasFormat 1203275.bibtex.
- aggregation hasFormat 1203275.csv.
- aggregation hasFormat 1203275.dc.
- aggregation hasFormat 1203275.didl.
- aggregation hasFormat 1203275.doc.
- aggregation hasFormat 1203275.json.
- aggregation hasFormat 1203275.mets.
- aggregation hasFormat 1203275.mods.
- aggregation hasFormat 1203275.rdf.
- aggregation hasFormat 1203275.ris.
- aggregation hasFormat 1203275.txt.
- aggregation hasFormat 1203275.xls.
- aggregation hasFormat 1203275.yaml.
- aggregation isPartOf urn:issn:0022-538X.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "O mannosylation of α-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function".
- aggregation abstract "alpha-Dystroglycan (alpha-DG) was identified as a common receptor for lymphocytic choriomeningitis virus (LCMW) and several other arenaviruses including the human pathogenic Lassa fever virus. Initial work postulated that interactions between arenavirus glycoproteins and alpha-DG are based on protein-protein interactions. We found, however, that susceptibility toward LCMV infection differed in various cell lines despite them expressing comparable levels of DG, suggesting that posttranslational modifications of alpha-DG would be involved in viral receptor function. Here, we demonstrate that glycosylation of alpha-DG, and in particular, 0 mannosylation, which is a rare type of O-linked glycosylation in mammals, is essential for LCMV receptor function. Cells that are defective in components of the O-mannosylation pathway showed strikingly reduced LCMV infectibility. As defective O mannosylation is associated with severe clinical symptoms in mammals such as congenital muscular dystrophies, it is likely that LCMV and potentially other arenaviruses may have selected this conserved and crucial posttranslational modification as the primary target structure for cell entry and infection.".
- aggregation authorList BK759383.
- aggregation endPage "14308".
- aggregation issue "22".
- aggregation startPage "14297".
- aggregation volume "79".
- aggregation aggregates 1203284.
- aggregation isDescribedBy 1203275.
- aggregation similarTo JVI.79.22.14297-14308.2005.
- aggregation similarTo LU-1203275.