Al. Lopata et al., CHARACTERISTICS OF HYPERSENSITIVITY REACTIONS AND IDENTIFICATION OF AUNIQUE 49 KD IGE-BINDING PROTEIN (HAL-M-1) IN ABALONE (HALIOTIS-MIDAE), Journal of allergy and clinical immunology, 100(5), 1997, pp. 642-648
Background: There is a paucity of published data on the clinical prese
ntation and the nature of the allergens involved in hypersensitivity t
o mollusks. This study reports the clinical and immunologic findings i
n 38 patients with reported immediate and delayed adverse reactions to
abalone (Haliotis midae, Class Gastropoda). Methods: Patients were re
cruited as part of a South African seafood allergy survey, Allergic sy
mptoms were assessed by a self-administered questionnaire, A total of
38 patients with abalone sensitivity were recruited, Specific IgE resp
onses to abalone and other mollusks were studied by using RAST and inh
ibition ELISAs, Skin prick tests and lymphocyte proliferation assays m
ere also performed on several of the subjects, Allergenic components o
f Haliotis midae were identified with Western blotting. Results: Twent
y five of the 38 patients in the study were first seen with immediate
symptoms, and 13 had delayed reactions. Seventeen of the sera tested w
ere RAST positive. Skin prick tests responses with abalone extract mer
e positive in all subjects with positive RAST responses (n = 8) and in
6 of 13 subjects with negative RAST responses. Five of the subjects w
ith positive RAST responses had positive results on Western blotting a
nd demonstrated binding to two major allergens with molecular weights
of 38 and 49 kd. The 49 kd IgE-binding protein has been designated as
Hal-m-1. Conclusions: Abalone allergens are heat-stable proteins,vith
molecular weights of 38 and 49 kd, later designated as Hal-m-1 accordi
ng to International Union of Immunological Societies allergen nomencla
ture regulation. Our studies indicate a clear clinical and immunologic
heterogeneity in patients reactive to abalone.