| Title: | A high proportion of anti-peptide antibodies recognize foot-and-mouth disease virus particles. |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1012422 |
| landingPage: |
http://www.iedb.org/assay/1495836 |
| type: |
Literature
|
| publicationVenue: |
Immunology
|
| dates: |
1988
|
| study type: | b cell assays |
| subject species: | Foot-and-mouth disease virus (strain O1) (O1BFS 1860) |
| fullName: |
N R Parry
A Syred
D J Rowlands
F Brown
|
| method: |
ELISA
|
| name: |
A high proportion of anti-peptide antibodies recognize foot-and-mouth disease virus particles.
|
| description: |
Sera from guinea pigs immunized with the uncoupled epitope, the epitope-KLH conjugate, or the longer peptides 135-160C-KLH or 130-160C (YNGECRYSRNAVPNLRGDLQVLAQKVARTLP), reacted with the epitope, synthesized with a C-terminal Cys residue. Absorption of antisera to 141-160C, 135-160C, or 130-160C with 140S virus particles reduced binding to the epitope by 31-38%, 60%, and 70%, respectively. Immunization with a fusion protein composed of four copies of VP1 amino acids 137-162 linked to beta-galactosidase also elicited an antiserum that bound the homologous peptide. Binding activity of this antiserum was reduced 41-66 % by absorption with 140S virus particles.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |