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identifier: 1268688
description:
epitope description:QYNLAFSDRQSAQ
antigen name:Pre-glycoprotein polyprotein GP complex
host organism:Mus musculus
antibody name:197.1 and 2.11.10
aggregation:
instance of dataset
availability:
available
primaryPublications: 2474891
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.

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