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identifier: 1495836
description:
epitope description:VPNLRGDLQVLAQKVARTLP
antigen name:Polyprotein
host organism:Cavia porcellus Duncan-Hartley
aggregation:
instance of dataset
availability:
available
primaryPublications: 2844657
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.

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