O mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• O mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• Imperiali M., Thoma C., Pavoni E., Brancaccio A., Callewaert N., Oxenius A. (2005)
  O mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function
  in Journal of virology (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Imperiali M., Thoma C., Pavoni E., Brancaccio A., Callewaert N., Oxenius A. (literal)

Pagina inizio

• 14297 (literal)

Pagina fine

• 14308 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 79 (literal)

Rivista

• Journal of virology (Rivista)

Note

• Scopu (literal)
• ISI Web of Science (WOS) (literal)
• PubMe (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Imperiali M., Thoma C., Callewaert N., Oxenius A.: Institute for Microbiology, ETH Zurich; Brancaccio A., ICRM-CNR; Pavoni E., UCSC (literal)

Titolo

• O mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function (literal)

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. (literal)

Prodotto di

• Modellistica molecolare di proteine legate a processi patologici (PM.P01.026.002) (Modulo)
• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)

Autore CNR

• ANDREA BRANCACCIO (Unità di personale interno)

Incoming links:

Autore CNR di

• ANDREA BRANCACCIO (Unità di personale interno)

Prodotto

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)
• Modellistica molecolare di proteine legate a processi patologici (PM.P01.026.002) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Journal of virology (Rivista)