BACKGROUND: With the increase in commercial vegetable production in greenhouses, occupational sensitization to bumblebee venom is becoming more common. Studies using sera from subjects thus sensitized allow evaluation of the allergenic specificity of bumblebee sensitization. OBJECTIVE: The purposes of this study were to determine the degree of species group specificity of bumblebee venom allergens in sera of @entity56 @entity1 and to investigate the structural basis of this specificity. METHODS: Allergens were purified from bumblebee venom, studied serologically by direct binding and inhibition techniques, and characterized by enzyme analysis and @entity535 sequencing. Three-dimensional models of the phospholipases were constructed and analyzed. RESULTS: @entity20993 venom contains phospholipase A(2), venom protease, hyaluronidase, and acid phosphatase allergens. The protease and phospholipase A(2) allergens contain IgE-reactive epitopes that are different from those seen in Bombus pennsylvanicus, a North American species. Bumblebee phospholipase A(2) is only 53% identical to @entity5157 phospholipase A(2). The results of 3-dimensional modeling are consistent with the immunologic observations. CONCLUSIONS: @entity1 with primary bumblebee sensitization should be diagnosed and treated with venom from the appropriate species group of bumblebees. Bumblebee venom phospholipase A(2) and protease are antigenically distinct from @entity5157 venom proteins. There are significant species group-specific epitopes on bumblebee venom proteins.

Occupational allergy to bumblebees: allergens of XXXX .

@entity1 :: ('9606', 'Species') :: ['Patients', 'patients'] @entity535 :: ('CHEBI:33704', 'Chemical') :: ['amino acid'] @entity20993 :: ('30195', 'Species') :: ['Bombus terrestris'] @entity56 :: ('MESH:D004342', 'Disease') :: ['allergic'] @entity5157 :: ('7460', 'Species') :: ['honeybee']
@entity20993 :: (30195,Species) :: ['Bombus terrestris']
