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Introduction

The major Bee Venom (BV) allergen is the phospholipase A2 (PLA). Phospholipases A2 (PLA2s) are enzymes that release fatty acids from the second carbon group of glycerol. PLA2 enzymes are commonly found in mammalian tissues as well as insect venom. The venom is largely composed of melittin, which is a stimulant of PLA2. Due to the increased presence and activity of PLA2 resulting from a snake or insect bite, arachidonic acid is released from the phospholipid membrane disproportionately. As a result, inflammation and pain occur at the site (1).

Figure 1: Phospholipid with phospholipase cleavage sites (in orange)

Epitopes

PLA 1 (our counting), is the sequence of one of the most immunogenic epitopes of PLA protein, amino acids 113-124.

Figure 2: 62 sequentially overlapping dodecapeptides (12 aa) representing the full length of the PLA molecule. The highest immunogenic response was of the 81-92 and 113-124 epitopes (2).

References

(1) Müller, Ulrich, et al. "Successful immunotherapy with T-cell epitope peptides of bee venom phospholipase A2 induces specific T-cell anergy in patients allergic to bee venom." Journal of allergy and clinical immunology 101.6 (1998): 747-754.‏

(2) Carballido, J. M., et al. "T cell epitope specificity in human allergic and nonallergic subjects to bee venom phospholipase A2." The Journal of Immunology 150.8 (1993): 3582-3591.‏

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