Immunological Data Discovery Index
Immunological Data Discovery Index
| identifier: | 1831442 |
| description: |
epitope description:Chain A: N47, E49, A51, N52, E133, N134, I135, K136, Y137, E138, F167, S168: Chain B: K310, F311, L312, Q328, N368, K370
antigen name:Genome polyprotein
host organism:Homo sapiens
antibody name:CR4354
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| aggregation: |
instance of dataset
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| availability: |
available
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| primaryPublications: |
20956322 |
| authorizations: |
registration not required
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| accessURL: |
http://www.iedb.org/reference/1021195 |
| landingPage: |
http://www.iedb.org/assay/1831442 |
| type: |
Literature
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| publicationVenue: |
Proc Natl Acad Sci U S A
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| dates: |
2010
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| study type: | b cell assays |
| subject species: | West Nile virus |
| fullName: |
Bä
rbel Kaufmann
Matthew R Vogt
Jaap Goudsmit
Heather A Holdaway
Anastasia A Aksyuk
Paul R Chipman
Richard J Kuhn
Michael S Diamond
Michael G Rossmann
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| method: |
electron microscopy
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| name: |
Neutralization of West Nile virus by cross-linking of its surface proteins with Fab fragments of the human monoclonal antibody CR4354.
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| description: |
This is, as it is called in the paper, the epitope X1 formed by interaction of Fab with the antigen chains A and B [PDB: 3IYW]
it is also a part of a larger epitope X2 discussed in the paper.
The structure of the CR4354 Fab complexed with WNV virions was determined by cryoEM. The epitope residues contacted by the Fab on the envelope glycoprotein were determined by fitting the atomic coordinates of the E glycoprotein and of CR4354 [PDB: 3N9G] into the cryoEM density. On asymmetric unit contained three E molecules and two Fab molecules. Each CR4354 Fab contacted two neighboring E molecules. The epitopes, called X1 and X2 in the paper, are different. This assay is for the epitope X1.
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| name: |
iedb
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| homePage: |
http://www.iedb.org |
