Stinging insect allergy--treatment failures.
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Specific IgE antibodies and total antibodies reacting with bee venom and yellow jacket venom were measured in sequential serum samples of insect-sensitive individuals. Venom-specific IgE decreased as a function of time and was not significantly affected by treatment with whole body extracts. There was no stimulation of total antibodies reacting with bee venom phospholipase A2 (PLA) following treatment with whole bee body extracts. These studies suggest that as measured by these parameters, whole body insect extracts used in the usual recommended doses are immunologically ineffective antigens.
Recent reports have indicated that venoms may be more beneficial than whole body extracts for the diagnosis and treatment of Hymenoptera sensitive patients. These studies were undertaken to determine the cross-reactivity among the vespid venoms. Eighteen patients who were anaphylactically sensitive to vespid venoms were studied using in vitro leukocyte histamine release. The results (venom concentration for 50% histamine release) were analyzed by linear regression analysis; there was no allergenic cross-reactivity between any of the venoms, except for a modest association between yellow hornet and white hornet venom. In spite of this result 13 of the 18 patients studied were sensitive to three or four of the venoms tested. There is no clear explanation for this observation, but it suggests the existence of multiple major allergens in the vespid venoms, some of which are cross-reactive. Since immunotherapy with inappropriate proteins may lead to the development of IgE and the possibility of clinical sensitivity and since the majority of patients were not sensitive to all venom preparations, we suggest that appropriate diagnostic studies be carried out before the institution of therapy.
In order to determine the proteins of major allergenic importance in honeybee venom (Apis mellifera) it was chromatographed on G-50 Sephadex. The four major protein peaks eluted were identified as hyaluronidase, phospholipase, melittin, and apamin. Testing these preparations on the leukocytes of 6 honeybee-sensitive patients, with the in vitro method of histamine release, revealed that all individuals were most sensitive to phospholipase A. IgE antibodies against phospholipase A (RAST) were found in the sera of honeybee-sensitive patients and IgG antibodies to this venom component were found in the sera from beekeepers and venom-treated patients. Melittin appeared to be allergenic in several patients, but the results were variable and were possibly due to contamination with phospholipase. All patients were insensitive to the hyaluronidase and apamin preparations. We conclude that phospholipase A is the major allergen of honeybee venom and, since this protein is readily available, it should be useful for diagnostic and therapeutic studies as well as for the standardization of materials used in the management of honeybee-sensitive patients.
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The relative diagnostic value of ST and RAST was evaluated in 97 patients with BSH. Eighteen patients had LRs, 79 showed SRs including 18 with urticaria, 26 had bronchospasm, and 35 had anaphylactic shock. ST but not the RAST reactivity was strongly related to the severity of the clinical reaction (p less than or equal to 0.001) and found superior to the RAST in identifying patients with SRs in whom venom therapy was indicated.
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