Analysis of immune responses in the sheep to synthetic peptides of foot-and-mouth disease virus using ovine polyclonal and monoclonal antibodies.

Title:

Analysis of immune responses in the sheep to synthetic peptides of foot-and-mouth disease virus using ovine polyclonal and monoclonal antibodies.

identifier:	1484530
description:	epitope description:CCRHKQKIVAPVKQTLPPSVPNLRGDLQVLAQKVARTPCG host organism:Ovis aries antibody name:3E4, 5E11, 4C6-D6, 4C6-E5, 1C9, 7G7, 5D5, 5D9, 5F8, 6B6, 2E6, 6C11
aggregation:	instance of dataset
availability:	available
primaryPublications:	1690176

study type:	b cell assays
subject species:

fullName:	J N Flynn G D Harkiss R DiMarchi

method:	antigen inhibition

name:	Analysis of immune responses in the sheep to synthetic peptides of foot-and-mouth disease virus using ovine polyclonal and monoclonal antibodies.
description:	The epitope is a construct of FMDV VP1 residues 200-213 joined by a Pro-Pro-Ser linker to residues 141-158 and with a dicysteine at the N-terminus and Pro-Cys-Gly at the C-terminus. The epitope sequence is from reference cited: DiMarchi et al. (1986) Science. 232: 639-641. [PMID: 3008333] The epitope inhibited epitope-specific mAbs from binding to the epitope. MAbs 5D9, 5F8, 6B6, 2E6, and 6C11 reacted with the epitope and with the shorter 21-residue peptide (VPNLRGDLQVLAQKVARTPCG), whereas mAbs 3E4, 5E11, 4C6-D6, 4C6-E5, 1C9, 7G7, and 5D5 reacted only with the epitope. The binding of mAbs 3E4, 5E11, 4C6-D6, 1C9, 7G7, and 5D5 to the epitope was not inhibited by the 19- or 21-residue peptides that compose the epitope.The authors conclude that these mAbs were binding to unique epitopes not present on the shorter peptides.

name:	iedb
homePage:	http://www.iedb.org

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