Table 5

Natural variants of the DQ2-γ-I epitope
No. 4- 3- 2- 1- 1 2 3 4 5 6 7 8 9 1+ 2+ 3+ 4+ Genome Group
1 Q P
    Q
Q P
    Q
Q S F P Q Q
    Q
Q P L I ABD 3, 7
2 Q P
    Q
Q P
    Q
Q S F P Q
    Q
    Q
    Q
L M I ABD 5
3* Q P
    Q
Q P
    Q
Q P F P Q Q
    Q
Q P L I ABD, Ab 6
4 Q P
    Q
Q P
    Q
Q S F P Q Q
    Q
Q P A I ABD 5
5 Q P
    Q
Q P
    Q
Q S F P Q
    Q
Q P S L I D, S 12, 11
6 Q P
    Q
Q P Q Q S S P Q
    Q
    Q
    Q
L L I S 1, 2
7 Q S
    Q
Q P Q Q S S P Q
    Q
    Q
    Q
L L I ABD, S 3
8 Q P Q Q S Q Q S S P Q
    Q
    Q
    Q
L L I S 4
9 Q P
    Q
Q P
    Q
Q S F P Q
    Q
    Q
    Q
W M I ABD, S 5
10 Q P
    Q
Q P
    Q
Q S F P Q Q
    Q
R P
    F
I ABD, S, D 8, 9
11 Q P
    Q
Q P
    Q
Q S F P Q Q
    Q
R S
    F
I ABD, D 9
12 Q P
    Q
Q P
    Q
Q S F P Q
    Q
Q P P
    F
I ABD, D 10
13 Q P
    Q
Q P
    Q
Q S F P Q
    Q
Q P P L I Ab 7

Natural variants of the DQ2-γ-I epitope, including the 9-mer core motif and four flanking amino acid positions on both sides of the core, found among genomic sequences of T. monococcum subspec. monococcum (Ab genome), Ae. speltoides var. speltoides (S-genome) and Ae. tauschii (D-genome) and T. aestivum transcripts (ABD genome). Group = Neighbor-Joining topology group of the epitope motif (see Figure 2). Glutamine residues that are a primary targets for the enzyme tissue transglutaminase are bold underlined (

) in QxP target sites whereas moderate target sites are depicted in italics, underlined ( ) [13,14]. Cleavage sites: R in bold, trypsin; underlined, chymotrypsin-high specificity; cleavage occurs at the right side (C-terminal direction) of the marked amino acid.

Salentijn et al.

Salentijn et al. BMC Genomics 2012 13:277   doi:10.1186/1471-2164-13-277

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