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Identification and characterization of the antigenic site (epitope) on bovine β ‐lactoglobulin: common residues in linear and conformational epitopes
Author(s) -
Li Xin,
Yuan Shuilin,
He Shengfa,
Gao Jinyan,
Chen Hongbing
Publication year - 2015
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.7033
Subject(s) - epitope , linear epitope , panning (audio) , peptide , conformational epitope , chemistry , phage display , antigen , computational biology , biochemistry , biology , immunology , paleontology , zoom , lens (geology)
BACKGROUND β ‐Lactoglobulin is recognised as one of major allergens in milk and its epitopes include linear and conformational epitopes contributed to milk allergy. RESULTS In our work, two types of epitopes have been identified. Linear epitopes identified by using SPOT™ peptide arrays approach and three common peptide sequences AA77 –82 ( KIPAVF ), AA126 –131 ( PEVDNE ) and AA142 –147 ( ALPMHI ) were obtained by reacting with specific sera from two rabbits. At the same time, mimotopes were screened by the panning of a phage display peptide library and the corresponding conformational epitopes were calculated by the web tool of Peptiope server with Mapitope algorithm. Three conformational epitopes against two specific sera were identified, in which there were 15 common residues as well and located in the different position and appeared mainly as an α‐helix. CONCLUSION Common residues on the linear and conformational epitopes were identified in the first time, respectively, which could be regarded as informative epitopes for detection of allergen in dairy products. © 2014 Society of Chemical Industry