Recombinant Human Anti-Major allergen Bet v 1 Antibody (M0418) (CAT#: PABL-269)

Figure 1 Binding specificity of novel scFv selected on Bet v 1 as determined by phage-ELISA on a panel of different allergens and BSA. All scFv are highly Bet v 1-specific and show no detectable cross-reactivity.

Levin, M., Davies, A. M., Liljekvist, M., Carlsson, F., Gould, H. J., Sutton, B. J., & Ohlin, M. (2014). Human I g E against the major allergen B et v 1–defining an epitope with limited cross‐reactivity between different PR‐10 family proteins. Clinical & Experimental Allergy, 44(2), 288-299.

Figure 2 Reactivity profiling of the four scFv against the three naturally occurring isoforms Bet v 1.0101, Bet v 1.0102 and Bet v 1.0112 and the artificial isoforms Bet v 1.2744 (Bet v 1.0112 carrying mutations N28T, L32Q, E45S and P108G) and Bet v 1.2595 (Bet v 1.0112 carrying mutations Y5V, E42S, E45S, N78K, K103V, K123I, K134E and D156H and an additional asparagine at position 160).

Levin, M., Davies, A. M., Liljekvist, M., Carlsson, F., Gould, H. J., Sutton, B. J., & Ohlin, M. (2014). Human I g E against the major allergen B et v 1–defining an epitope with limited cross‐reactivity between different PR‐10 family proteins. Clinical & Experimental Allergy, 44(2), 288-299.

Figure 3 Peptide mapping of epitopes recognized by Bet v 1-specific scFv-Fcε fusion proteins and reactivity profiling of IgE clone M0418.

A peptide encompassing residues I56 to D69 of Bet v 1.0101, recognized by the two sequence-related IgE clones M0418 and B14, and an additional peptide spanning residues G26 to S39, recognized by B10, had been identified. Inhibition of binding of these scFv-Fcε to immobilized Bet v 1 by respective peptides confirmed the reactivity of these scFv-Fcε to these parts of the allergen (a). Alanine-scanning modifications of residues within this sequence defines the importance of each residue for reactivity with M0418 (b). Further, reactivity profile of M0418 against the identified Bet v 1.0101 peptide I56 to D69 and modified versions thereof was performed (c). Modifications include some of those found in isoforms of Bet v 1, in homologues of Bet v 1 found in other Betula species, or in PR-10 family proteins of other plant species. Critical amino acid differences that explain an inability of M0418 to bind different isoforms/homologues are apparent, as illustrated by the lack of reactivity (d) against Mal d 1.0108 and Aln g 1.0101 (both of which among other differences carry the F62S mutation).

Levin, M., Davies, A. M., Liljekvist, M., Carlsson, F., Gould, H. J., Sutton, B. J., & Ohlin, M. (2014). Human I g E against the major allergen B et v 1–defining an epitope with limited cross‐reactivity between different PR‐10 family proteins. Clinical & Experimental Allergy, 44(2), 288-299.