A new recombinant mosquito salivary allergen, rAed a 2: allergenicity, clinical relevance, and cross-reactivity

Authors


Dr Z. Peng
Department of Pediatrics and Child Health
University of Manitoba
532 John Buhler Research Centre
715 McDermot Ave.
Winnipeg R3E 3P5
MB, Canada

Abstract

Background:  Mosquito salivary proteins cause allergic reactions in humans. The allergenicity, clinical relevance, and species cross-reactivity of a new 37-kDa recombinant mosquito (Aedes aegypti) salivary allergen, rAed a 2, were evaluated.

Methods:  rAed a 2 was expressed using a baculovirus/insect cell system and purified. Its allergenicity was examined using an enzyme-linked immunosorbent assay (ELISA), ELISA inhibition tests, immunoblots, and skin tests. Epicutaneous tests with the allergen, mosquito whole body extracts, and mosquito bite tests were performed on 48 volunteers. Serum rAed a 2-specific immunoglobulin E (IgE) was measured in individuals with positive mosquito saliva-specific IgE and negative controls.

Results:  Both immunoblots and ELISAs demonstrated that rAed a 2 bound to the IgE of mosquito-allergic individuals. The binding could be inhibited by the addition of a natural mosquito preparation. Furthermore, rAed a 2 induced immediate and delayed skin reactions. Ten per cent of 31 participants with a positive mosquito bite test had positive skin reactions to rAed a 2, compared with 32% for mosquito whole body extract. None of the participants with a negative bite test showed positive reactions to either of the two extracts. Forty-three per cent of individuals with positive saliva-IgE had positive rAed a 2-IgE. rAed a 2 was a species-shared allergen, being present in the saliva of the 11 species studied.

Conclusions:  rAed a 2 has identical antigenicity and biologic activity to its native form. It can be used in the diagnosis of mosquito allergy, and is an important species-shared antigen.

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