| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1000847 |
| landingPage: |
http://www.iedb.org/assay/1268688 |
| type: |
Literature
|
| publicationVenue: |
Virology
|
| dates: |
1989
|
| study type: | b cell assays |
| subject species: | Lymphocytic choriomeningitis virus (strain Armstrong) (clone 4) |
| fullName: |
K E Wright
M S Salvato
M J Buchmeier
|
| method: |
immuno staining
|
| name: |
Neutralizing epitopes of lymphocytic choriomeningitis virus are conformational and require both glycosylation and disulfide bonds for expression.
|
| description: |
Monoclonal antibodies generated against LCMV were used to define two neutralizing epitopes, A and D, of the surface glycoprotein (GP1).
To investigate whether epitope A and D were dependent on N-linked glycosylation, LCMV Arm 4 was treated with tunicamycin (TUN) in culture. Epitopes A and D were detected by fluorescence on LCMV-infected BHK cells. However, in the presence of TUN, neither epitope A or D were detectable, indicating their dependence on N-linked glycosylation. The absence of epitope D in TUN-treated infected cells was confirmed by immunoprecipitation. In a separate experiment, it was found that the cotranslational addition of carbohydrates is required for proper folding for these epitopes, but not for maintaining the protein conformation. The addition of one extra N-linked carbohydrate disrupted reactivity to epitope D.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |