| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1003429 |
| landingPage: |
http://www.iedb.org/assay/1361485 |
| type: |
Literature
|
| publicationVenue: |
Protein Eng
|
| dates: |
1997
|
| study type: | b cell assays |
| subject species: | Hepatitis B virus subtype ayw |
| fullName: |
B Vulliez-le Normand
F A Saul
P Martineau
F Lema
M Hofnung
G A Bentley
|
| method: |
antigen inhibition
|
| name: |
Maltodextrin-binding protein hybrids carrying epitopes from the preS2 region of hepatitis B virus: expression, antibody-binding and preliminary crystallographic studies.
|
| description: |
The B-epitope was inserted as various internal positions of the carrier protein maltrodextrin-binding protein (MBP) and was flanked on both ends by amino acids arising from the construction of the expression plasmid. Different binding affinities of the epitope to the mAb was said to probably reflect a combination of factors such as accessibility of the epitope to the mAb and the influence of the carrier protein (MBP) upon its conformation and flexibility. When the epitope and a T-cell epitope (MQWNSTTFHQTLQ, HBV preS 120-132) fused at the N-terminal of the epitope were separately inserted at the same position in MBP, higher antibody binding was observed with the fusion construct than with the B-epitope alone. Similar results were obtained when the hybrid was immobilized on the ELISA plate to compete for mAb binding to viral particlesor the preS2 peptide 120-145 (serotype ayw).
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |