Screening of transgenic proteins expressed in transgenic food crops for the presence of short amino acid sequences identical to potential, IgE – binding linear epitopes of allergens

Table 5 Identical sequences between transgenic- and allergenic proteins of special interest

Transgenic protein (1)	Identical peptide	Allergens (2)	Remark
Insecticidal protein Cry1Ac (Bacillus thuringiensis kurstaki HD-73)	GNAAPQ GSTGITI	Cedar pollen allergens Cup a 1, Jun a 1, Jun o 1, Juniperus virginiana 1–1, and Juniperus virginiana 1–2	Two sequences shared with same allergens, potential crosslinking of IgE if bound by both sequences
Papaya Ringspot Virus coat protein	EKQKEK	Nematode allergen ABA-1 (Ascaris suum, A. lumbricoides)	Sequence predicted to be antigenic determinant of allergenic protein (Figure 4)
Acetolactate synthase (GH50 mutant, Arabidopsis thaliana)	KVLENR (3)	Shrimp allergen Met e 1 Lobster allergens Hom a 1 and Pan s 1 Crab allergen Cha f 1	KVLENR is part of 15-mer peptides that are recognised by sera from allergic patients [28, 29]
Glyphosate oxidoreductase (Achromobacter LBAA)	LAEEAD	Shrimp allergen Met e 1 Lobster allergens Hom a 1 and Pan s 1 Crab allergen Cha f 1 Fish parasite allergen Ani s 3	LAEEAD is part of 9-mer peptide from the shrimp tropomyosin allergen Pen i 1 that is bound by sera from shrimp allergic patients [26, 27] (4)

(1) Accessions: Cry1Ac: gi117547; PRV CP: gi593497; ALS: gi124372; GOX: gi1252836 (2) Accessions: Cup a 1: gi19069497, gi9087167, gi6562326; Jun a 1: gi9087152, gi4138877, gi4138879; Jun o 1: gi15139849; Juniperus virginiana major pollen allergens 1–1 and 1–2: gi8843917, gi8843921; ABA-1: gi2735108, gi2735110, gi2735112, gi2735114, gi2735116, gi2735118, gi2970629, gi7494507; Met e 1: gi607633, gi6094504; Hom a 1: gi14285796; Pan s 1: gi3080761, gi14285797; Cha f 1: gi7024506, gi14285800; Ani s 3: gi14423976 (3) Sequence KVLENR immediately flanks the highest peak in the antigenicity plot of acetolactate synthase. This peak is located between the arginine residu (KVLEN R) and the adjacent C-terminal residue (4) Sequence LAEEAD is also part of two 15-mer peptides from the shrimp allergen Pen a 1 tested for sera binding. One peptide is bound by sera from allergic individuals, whereas the other peptide is not [28].