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. 2011 Mar 24;286(20):17569–17578. doi: 10.1074/jbc.M110.194878

TABLE 1.

Mutated recombinant Mal d 1 variants

Mutated variants Amino acid substitutionsa
Mut-2782b,c,d I43N, L44I, D47N, K70R, E76H
Mut-2781b,d,e,f I43N, L44I, D47N, G65K, K70R, E76H
Mut-2762b,f,g E12V, P16A, S107T, G108P, +109D, S110G, K152L, P155S
Mut-2760f,h N28T, K32Q, E45S

a Amino acid substitutions were introduced into Mal d 1 (Q8L6K9).

b Residues in Mal d 1 were substituted to residues present in corresponding positions in Bet v 1.

c All five mutations in Mut-2782 are located within the BV16 antibody footprint illustrated in Fig. 2.

d Mut-2781 and Mut-2782 were tested along with rBet v 1 and rMal d 1 in Biacore experiments with mAb BV16.

e In addition to the five mutations located within the BV16 antibody footprint, Mut-2781 contains an additional mutation G65K located outside the footprint as shown in Fig. 3B.

f Mut-2781, Mut-2762, and Mut-2760 were tested along with rBet v 1 and rMal d 1 in IgE-binding experiments with birch-allergic patient sera and in histamine release assays with blood from birch-allergic patients.

g (+109D) refers to the insertion of aspartic acid extending the length of the mutated molecule to 159 amino acid residues.

h Residues in Mal d 1 were substituted to residues not present in corresponding positions in Bet v 1.