Unique N-linked glycosylation of CasBrE Env influences its stability, processing, and viral infectivity but not its neurotoxicity.

Title

Unique N-linked glycosylation of CasBrE Env influences its stability, processing, and viral infectivity but not its neurotoxicity.

Creator

Renszel Krystal M; Traister Russell S; Lynch William P

Publisher

Journal of virology

Date

2013
2013-08

Description

The envelope protein (Env) from the CasBrE murine leukemia virus (MLV) can cause acute spongiform neurodegeneration analogous to that induced by prions. Upon central nervous system (CNS) infection, Env is expressed as multiple isoforms owing to differential asparagine (N)-linked glycosylation. Because

Subject

*Protein Processing; Animals; Canavan Disease/pathology/virology; DNA Mutational Analysis; env/genetics/*metabolism; Gene Products; Glycosylation; Leukemia Virus; Mice; Murine/genetics/*pathogenicity/*physiology; Post-Translational; Virulence; Virus Replication

Rights

Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).

URL Address

http://doi.org/10.1128/JVI.00392-13

Pages

8372–8387

Issue

15

Volume

87

Citation

Renszel Krystal M; Traister Russell S; Lynch William P, “Unique N-linked glycosylation of CasBrE Env influences its stability, processing, and viral infectivity but not its neurotoxicity.,” NEOMED Bibliography Database, accessed March 24, 2025, https://neomed.omeka.net/items/show/4540.