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J Gen Virol 89 (2008), 2713-2722; DOI 10.1099/vir.0.2008/004721-0

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Post-translational modification of {alpha}-dystroglycan is not critical for lymphocytic choriomeningitis virus receptor function in vivo

Mauro Imperiali1,{dagger}, Roman Spörri1, Jane Hewitt2 and Annette Oxenius1

1 Institute for Microbiology, ETH Zurich, 8093 Zürich, Switzerland
2 Institute of Genetics, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK

Correspondence
Annette Oxenius
oxenius{at}micro.biol.ethz.ch

{alpha}-Dystroglycan ({alpha}-DG) is a ubiquitously expressed molecule that has been identified as a cellular receptor for lymphocytic choriomeningitis virus (LCMV) and other arenaviruses. Recently, it was demonstrated that LCMV receptor function is critically dependent on post-translational modifications, namely glycosylation. In particular, it was shown that O-mannosylation, a rare type of mammalian O-linked glycosylation, is important in determining the binding of LCMV to its cellular receptor. All studies carried out so far showed a dependence on glycosylation in LCMV receptor function in vitro. This work extended these studies to two in vivo models of {alpha}-DG hypoglycosylation. The results confirm earlier findings on the in vitro dependence of carbohydrate modifications in LCMV receptor function. However, experiments in animal models showed that this dependence was only very weak in vivo. It is likely that alternative receptors or alternative entry pathways may account for this attenuated in vivo phenotype.

{dagger}Present address: Ospedale San Giovanni, Laboratorio di Chimica Clinica, 6500 Bellinzona, Switzerland.







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