| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1016119 |
| landingPage: |
http://www.iedb.org/assay/1691100 |
| type: |
Literature
|
| publicationVenue: |
Proc Natl Acad Sci U S A
|
| dates: |
1998
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
A L Rothermel
D C Altieri
|
| method: |
antigen inhibition
|
| name: |
High affinity cross-reacting mAb generated by minimal mimicry: implications for the pathogenesis of anti-nuclear autoantibodies and immunosuppression.
|
| description: |
The epitope inhibited the nuclear staining of Ku80 by mAb 2E1.The longer peptide 571-595(GGAHFSVSSLAEGSVTSVGSVNPAE) was also shown to inhibit the binding of mAb 2E1 to E2 protein by ELISA. MAb bound the epitope and the longer peptide 571-595 in a direct ELISA. MAb 2E1 recognizes three proteins E2, EPR-1, and Ku80. The epitope inhibited the binding of mAb 2E1 to E2 protein in a dose-dependent manner on EPR-1-negative Jurkat T cells. The epitope also inhibited the binding of mAb 2E1 to transfected cells expressing the EPR-1 epitope (residues 1-60) as a chimeric protein with intracellular adhesion molecule 1. The epitopes on the three proteins contain a minimal homology motif, FSXXXLA, in which X is a nonconserved amino acid.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |