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Identification of the Critical Amino Acid Residues of Immunoglobulin E and Immunoglobulin G Epitopes in α‐Lactalbumin by Alanine Scanning Analysis
Author(s) -
Yanjun Cong,
Shengyun Zhou,
Linfeng Li
Publication year - 2016
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/1750-3841.13425
Subject(s) - epitope , lactalbumin , immunoglobulin e , antibody , chemistry , alanine , amino acid , biochemistry , immunoglobulin g , microbiology and biotechnology , linear epitope , peptide sequence , biology , immunology , gene
α‐Lactalbumin represents one of the major allergens causing cow milk allergy. Few studies have clearly evaluated immunological relationships between immunoglobulin E (IgE) and immunoglobulin G (IgG)‐binding epitopes of α‐lactalbumin. IgE‐ and IgG‐binding epitopes were immunolabeled with individual sera from cow milk‐allergic patients. Alanine scanning of immunodominant epitopes was used to identify the critical amino acid (aa). Our initial data revealed Val 8 , Phe 9 , Arg 10 , Tyr 103 , Leu 105 , and His 107 were the critical aa for IgE‐binding epitope. The critical aa of IgG‐binding epitopes were Phe 9 , Leu 15 , Pro 24 , Trp 26 , and His 32 . This study will provide necessary information to alter the cDNA to encode a protein capable of activating milk‐specific T cells, but with reduced IgE‐ or IgG‐binding capacity.