| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1000844 |
| landingPage: |
http://www.iedb.org/assay/1212511 |
| type: |
Literature
|
| publicationVenue: |
Mol Immunol
|
| dates: |
1988
|
| study type: | b cell assays |
| subject species: | Rabies lyssavirus |
| fullName: |
L Bracci
G Antoni
M G Cusi
L Lozzi
N Niccolai
S Petreni
M Rustici
A Santucci
P Soldani
P E Valensin
|
| method: |
immuno staining
|
| name: |
Antipeptide monoclonal antibodies inhibit the binding of rabies virus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor.
|
| description: |
This sequence was selected because it corresponds to the region considered to contain the active site in homologous sequences of neurotoxins. Also, the NSRG tetrapeptide was predicted as a reverse turn by the Chou and Fasman method. Finally, the peptide corresponds to a peak in the hydrophilicity profile of rabies virus glycoprotein.
Monoclonal antibodies generated against the peptide-KLH conjugate were shown to recognize rabies virus-infected BHK21 cells. In additional assays, the monoclonal antibody was shown to be effective in inhibiting binding of rabies virus glycoprotein and alpha-bungarotoxin to acetylcholine receptors.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |