Increased HLA-DQ2-affinity of a synthetic gliadin peptide by acid-induced deamidation of glutamine residues.
Presentation of antigenic gliadin peptides by the HLA-DQ2 molecule is considered as a key event in celiac disease pathogenesis. Chemical deamidation of the side chains of glutamine residues might have a strong influence on gliadin peptide binding to the DQ2 molecule. Glutamine deamidation of A-gliadin peptide (45-56) under acidic conditions corresponding to the gastric environment was studied using RP-HPLC, Edman degradation, capillary electrophoresis and electrospray mass spectrometry. Deamidation resulted in peptides with increased DQ2-affinities as assessed in a cell-free binding assay.
Terreaux
C
C
Institute of Organic Chemistry, University of Tübingen, Germany.
Walk
T
T
van de Wal
Y
Y
Koning
F
F
Jung
G
G
Fleckenstein
B
B
D000577:Amides / Q000737:chemistry; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D019075:Electrophoresis, Capillary; D005973:Glutamine / Q000737:chemistry*; D006683:HLA-DQ Antigens / Q000378:metabolism*; D006868:Hydrolysis; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding
C116805:A-glidin peptide (45-56); D000577:Amides; D006683:HLA-DQ Antigens; C053186:HLA-DQ2 antigen; D010446:Peptide Fragments; D005973:Glutamine