epitope description:DRPVPY

host organism:Mus musculus

antibody name:SA-3

instance of dataset

available

registration not required

Literature

Proc Natl Acad Sci U S A

1997

S L Harris

L Craig

J S Mehroke

M Rashed

M B Zwick

K Kenar

E J Toone

N Greenspan

F I Auzanneau

J R Marino-Albernas

B M Pinto

J K Scott

calorimetry

Exploring the basis of peptide-carbohydrate crossreactivity: evidence for discrimination by peptides between closely related anti-carbohydrate antibodies.

Peptide selected from a random 6-mer library by an anti-carbohydrate antibody specific for the Group A Streptococcus cell-wall polysaccharide.

A streptavidin-immobilized peptide that includes the epitope is shown to be recognized by the mAb used for immunopanning in ELISA, but not by other 4 close related (in VH and VL sequence as well as in carbohydrate specificity) mAbs. The peptide is inferred to bind to the carbohydrate bidning site based on identical binding stoichiometries for the peptide and a CWPS derived oligosaccharide. Titration calorimetry affinity measurement reveals a 30- fold higher affinity than for that oligosaccharide. These results suggest that the antigenic mimicry observed for this and other crossreactive peptides is determined mainly by the binding sites of anti-carbohydrate Abs (including small differences between them), rather than by chemical similarity to the corresponding carbohydrate epitope. This mAb sequence is not deposited in current databases. Its V_H region sequence is EVKLEESGGGLVQPGGSMKLSCVASGFTFSNYWMDWVRQSPEKGLEWVAEIRLKSNNYATHYAESVKGRFTISRDDSKSSVYLQMNNLRAEDTGIYYCIDLAWFAYWGQGTLVTVSA, its V_L region sequence is DIVMTQAAFSNPVTLGTSASISCRSSKNLLHSNGITYLYWYLQRPGQSPQLLIYRVSNLASGVPNRFSGSESGTDFTLRISRVEAEDVGVYYCAQLLELPYTFGGGTKLEIK. The carrier was composed of DRPVPY-peptide (ADGADRPVPYGACG).

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