IgE-binding epitopes of a major heat-stable crustacean allergen

Details IgE-binding epitopes of a major heat-stable crustacean allergen IgE-binding epitopes of a major heat-stable crustacean allergen

1993-11-10

1995-09-12

Warden, Jill

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

514 15, 530326, 530328, C07K 706, C07K 708, A61K 3808, A61K 3810

Patent

active

054496691

ABSTRACT:
A major heat-stable shrimp allergen is characterized as a 34 kDa protein corresponding to shrimp tropomyosin. Two IgE binding epitopes of this allergen have the sequences FLAEEADRK (SEQ ID NO: 1) and MQQLENDLDQVQESLLK (SEQ ID NO: 2), respectively. Surprisingly, both antigenic and allergenic activities of the allergen were found to be associated with these two peptide fractions. A-a-id antibodies recognized this allergen as well as a homologous 34 kDa allergen from lobster, prawn and crab, indicating that these antibodies recognize major cross-reacting IgE binding epitopes common to crustacea. The two epitopes are useful in the diagnosis and/or treatment of allergies, particularly in the desensitization of individuals that are allergic to shrimp and other crustacea. Variants and subfragments of the two epitopes display allergenicity, as assessed by reaction with allergen-specific IgE obtained from shrimp-sensitive patients.

REFERENCES:
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Lipman et al. "Rapid and Sensitive Protein Similarity Searches", Science, 227:1435-1441 (1985).
Greaser et al. "Reconstitution of Troponin Activity from Three Protein Components", J. Biol. Chem., 246(13):4226-4233 (1971).
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Laemmli "Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4", Nature, 227:680-685 (1970).
Hoffman et al. "The Major Heat Stable Allergen of Shrimp", Annals of Allergy, 47:17-22 (1981).
Subba Rao et al. Abstract, Immunol. Methods, 57:71 (1983).

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