Table 1.

Variants of T cell epitopes present in oat avenins that are predicted to resist trypsin and chymotrypsin digestion.

T Cell Epitopes (Deamidated in Bold)	Epitope Variants (Amino Acid Differences Underlined) Present in Oat Avenins that Are Predicted to Resist Trypsin and Chymotrypsin Digestion
DQ2.5-glia-γ2 IQPEQPAQL (from wheat)	N  Q  P  Q  Q  Q  A  Q  F
	I  Q  P  Q  Q  L  P  Q  Y
DQ2.5-glutL2 FSQQQESPF (from wheat)	V  Q  Q  Q  Q  Q  Q  P  F
DQ2.5-hor-1 PFPQPEQPF (from barley)	P  Y  P  E  Q  Q  Q  P  F
DQ2.5-sec-1 PFPQPEQPF (from rye)	P  Y  P  E  Q  Q  Q  P  F
DQ2.5-ave-1a PYPEQEEPF (from oat)	P  Y  P  E  Q  Q  Q  P  I
DQ2.5-ave-1b PYPEQEQPF (from oat)	P  Y  P  E  Q  Q  Q  S  I
	P  Y  P  E  Q  Q  Q  Q  L

Perfect T cell epitopes from wheat, barley, and rye are not present in oat avenins, but variants with one, two, and three amino acid differences (underlined) can be found in avenin sequences. Of 89 proteins derived from genomic sequencing of 13 diploid, tetraploid and hexaploid Avena species, only these eight epitope variants resisted in silico trypsin and chymotrypsin proteolysis; none of these variants remained intact if pepsin was also added (adapted from Londono et al. [23]).