| identifier: | 1327533 |
| description: |
epitope description:beta-D-Araf-(1->2)-alpha-D-Araf-(1->5)-[beta-D-Araf-(1->2)-alpha-D-Araf-(1->3)]-alpha-D-Araf-(1->5)-alpha-D-Araf-yl group
antigen name:lipoarabinomannan
host organism:Mus musculus
antibody name:CS-35
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
12368438 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1002169 |
| landingPage: |
http://www.iedb.org/assay/1327533 |
| type: |
Literature
|
| publicationVenue: |
Microbiology
|
| dates: |
2002
|
| study type: | b cell assays |
| subject species: | Mycobacterium leprae |
| fullName: |
Devinder Kaur
Todd L Lowary
Varalakshmi D Vissa
Dean C Crick
Patrick J Brennan
|
| method: |
antigen inhibition
|
| name: |
Characterization of the epitope of anti-lipoarabinomannan antibodies as the terminal hexaarabinofuranosyl motif of mycobacterial arabinans.
|
| description: |
This structure constitutes the hexaarabinofuranosyl termini of the arabinan as found in mycolylarabinogalactan-peptidoglycan complex and lipoarabinomannan of the mycobacterial cell wall. The lipoarabinomannan used in this study was isolated from the from M.smegmatis, while the one used for immunizations was from M.leprae.
The synthetic Hexa-Araf oligosaccharide is able to inhibit the binding of the anti-LAM mAb CS-35 to Arabinogalactan (AG). The tetrasaccharides that represent the linear segments of this epitope (without either branch) are less or non-effective, implying the full hexasaccharide is involved in recognition. LAM itself is also a good inhibitor.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |