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EPITOPE MAPPING OF BUFFALO BETA‐LACTOGLOBULIN AGAINST RABBIT POLYCLONAL ANTIBODY FOLLOWING PHAGE DISPLAY TECHNIQUE
Author(s) -
LI XIN,
CHEN HONGBING,
TONG PING,
WEN XUEFANG
Publication year - 2012
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2010.00502.x
Subject(s) - epitope , panning (audio) , phage display , polyclonal antibodies , epitope mapping , linear epitope , antibody , antigen , mimotope , biology , microbiology and biotechnology , computational biology , chemistry , immunology , paleontology , zoom , lens (geology)
We aim to map immunoglobulin G (IgG)‐binding linear epitopes on buffalo β‐lactoglobulin by prediction through bioinformatics analysis and screening from phage library. Five possible regions on buffalo β‐lactoglobulin were predicted as epitope candidates by LaserGene software and web service. Six mimic epitope regions, AA14‐20, AA26‐32, AA36‐42, AA70‐80, AA82‐86 and AA149‐156 were obtained by the panning of phage display peptide library with specific rabbit sera against buffalo β‐lactoglobulin with AA70‐80 and AA149‐156 as the major ones. Compared with the results of prediction and panning, 30% of predicted epitope regions accorded with the ones by panning, however, the 40% of panned epitopes were not predicted by bioformatics analysis. Additionally, two rabbit IgG‐binding regions on buffalo β‐lactoglobulin, AA134‐143(EKFDKALKAL) and AA149‐156 (LAFNPTQL), were found not to be reported on bovine β‐lactoglobulin. PRACTICAL APPLICATIONS Molecular biology and biochemical techniques have considerably advanced the knowledge of allergens and supported the characterization of isoforms and the determination of the primary, secondary and tertiary structures of these proteins. It has been explained that allergic disease is induced by the following mechanisms: Exogeneous antigens are processed by endosomal proteases to peptides in antigen presenting cells, and are presented to T cells by appropriate major histocompatability complex class II molecules present on the cell surface. For understanding of the mechanism of allergy, allergen epitopes should be known. So here we aim to map the epitopes of buffalo β‐lactoglobulin.