Posttranslational modification of alpha-dystroglycan, the cellular receptor for arenaviruses, by the glycosyltransferase LARGE is critical for virus binding.

Details

Serval ID
serval:BIB_E34C3C5FE6D1
Type
Article: article from journal or magazin.
Collection
Publications
Title
Posttranslational modification of alpha-dystroglycan, the cellular receptor for arenaviruses, by the glycosyltransferase LARGE is critical for virus binding.
Journal
Journal of Virology
Author(s)
Kunz S., Rojek J.M., Kanagawa M., Spiropoulou C.F., Barresi R., Campbell K.P., Oldstone M.B.
ISSN
0022-538X (Print)
ISSN-L
0022-538X
Publication state
Published
Issued date
2005
Volume
79
Number
22
Pages
14282-14296
Language
english
Abstract
The receptor for lymphocytic choriomeningitis virus (LCMV), the human pathogenic Lassa fever virus (LFV), and clade C New World arenaviruses is alpha-dystroglycan (alpha-DG), a cell surface receptor for proteins of the extracellular matrix (ECM). Specific posttranslational modification of alpha-DG by the glycosyltransferase LARGE is critical for its function as an ECM receptor. In the present study, we show that LARGE-dependent modification is also crucial for alpha-DG's function as a cellular receptor for arenaviruses. Virus binding involves the mucin-type domain of alpha-DG and depends on modification by LARGE. A crucial role of the LARGE-dependent glycosylation of alpha-DG for virus binding is found for several isolates of LCMV, LFV, and the arenaviruses Mobala and Oliveros. Since the posttranslational modification by LARGE is crucial for alpha-DG recognition by both arenaviruses and the host-derived ligand laminin, it also influences competition between virus and laminin for alpha-DG. Hence, LARGE-dependent glycosylation of alpha-DG has important implications for the virus-host cell interaction and the pathogenesis of LFV in humans.
Keywords
Animals, Arenaviridae/metabolism, Arenaviridae/physiology, Base Sequence, Crosses, Genetic, DNA Primers, DNA-Directed RNA Polymerases/metabolism, Dystroglycans/metabolism, Female, Kinetics, Male, Mice, Mice, Inbred C57BL, N-Acetylglucosaminyltransferases/metabolism, Protein Processing, Post-Translational, Viral Proteins/metabolism
Pubmed
Web of science
Open Access
Yes
Create date
17/04/2013 12:56
Last modification date
20/08/2019 17:07
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