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The glycosylation status of the murine hepatitis coronavirus M protein affects the interferogenic capacity of the virus in vitro and its ability to replicate in the liver but not the brain.
- Source :
-
Virology [Virology] 2003 Aug 01; Vol. 312 (2), pp. 395-406. - Publication Year :
- 2003
-
Abstract
- The coronavirus M protein, the most abundant coronaviral envelope component, is invariably glycosylated, which provides the virion with a diffuse, hydrophilic cover on its outer surface. Remarkably, while the group 1 and group 3 coronaviruses all have M proteins with N-linked sugars, the M proteins of the group 2 coronaviruses [e.g., mouse hepatitis virus (MHV)] are O-glycosylated. The conservation of the N- and O-glycosylation motifs suggests that each of these types of carbohydrate modifications is beneficial to their respective virus. Since glycosylation of the M protein is not required for virus assembly, the oligosaccharides are likely to be involved in the virus-host interaction. In order to investigate the role of the M protein glycosylation in the host, two genetically modified MHVs were generated by using targeted RNA recombination. The recombinant viruses carried M proteins that were either N-glycosylated or not glycosylated at all, and these were compared with the parental, O-glycosylated, virus. The M protein glycosylation state did not influence the tissue culture growth characteristics of the recombinant viruses. However, it affected their interferogenic capacity as measured using fixed, virus-infected cells. Viruses containing M proteins with N-linked sugars induced type I interferons to higher levels than viruses carrying M proteins with O-linked sugars. MHV with unglycosylated M proteins appeared to be a poor interferon inducer. In mice, the recombinant viruses differed in their ability to replicate in the liver, but not in the brain, whereas their in vivo interferogenic capacity did not appear to be affected by their glycosylation status. Strikingly, their abilities to replicate in the liver correlated with their in vitro interferogenic capacity. This apparent correlation might be explained by the functioning of lectins, such as the mannose receptor, which are abundantly expressed in the liver but also play a role in the induction of interferon-alpha by dendritic cells.
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
Coronavirus M Proteins
Formaldehyde
Gene Expression Regulation, Viral
Genetic Engineering
Glycosylation
Interferon Type I metabolism
Mice
Mice, Inbred Strains
Murine hepatitis virus genetics
Murine hepatitis virus growth & development
Murine hepatitis virus pathogenicity
Mutation genetics
Phenotype
Viral Matrix Proteins genetics
Brain virology
Liver virology
Murine hepatitis virus physiology
Viral Matrix Proteins metabolism
Virus Replication
Subjects
Details
- Language :
- English
- ISSN :
- 0042-6822
- Volume :
- 312
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Virology
- Publication Type :
- Academic Journal
- Accession number :
- 12919744
- Full Text :
- https://doi.org/10.1016/s0042-6822(03)00235-6