| identifier: | 1370356 |
| description: |
epitope description:EEEEE + D-aa(1, 2, 3, 4, 5)
antigen name:Other Bacillus anthracis (anthrax bacterium) protein
host organism:Mus musculus BALB/c
antibody name:F24F2, F24G7, F26G3, F26G4, F30D1
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| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
17060470 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1003642 |
| landingPage: |
http://www.iedb.org/assay/1370356 |
| type: |
Literature
|
| publicationVenue: |
Infect Immun
|
| dates: |
2007
|
| study type: | b cell assays |
| subject species: | Bacillus anthracis |
| fullName: |
Thomas R Kozel
Peter Thorkildson
Suzanne Brandt
William H Welch
Julie A Lovchik
David P AuCoin
Julpohng Vilai
C Rick Lyons
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| method: |
quenching
|
| name: |
Protective and immunochemical activities of monoclonal antibodies reactive with the Bacillus anthracis polypeptide capsule.
|
| description: |
The epitope is a peptide-like structure where the D-Glutamic acid residues are linked in amide bonds between the amino group and the gamma-carboxyl group instead of the alpha-carboxyl. The B.anthracis capsule antigen is a polymer of D-glutamic acid residues where the peptide bond is made via the gamma-carboxyl group. It is enzymatically synthesized.
The interaction with poly-gamma-D-glutamic acid (gammaDPGA) was determined by triptophan fluorescence quenching analysis. These mAbs provided protection following passive transfer to animals that were further challenged with B. anthracis spores. Also a non-protective IgG1 mAb recognized the gammaDPGA.
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| name: |
iedb
|
| homePage: |
http://www.iedb.org |