Structural, immunological and functional properties of natural recombinant Pen a 1, the major allergen of Brown Shrimp, Penaeus aztecus

Abstract

Recombinant Pen a 1 and natural Pen a 1 are structurally and immunologically identical and rPen a 1 may be used as the basis for component-resolved diagnosis and the generation of modified shrimp tropomyosin for allergen-specific immunotherapy. The results of the animal studies indicate that C3H/HeJ mice that were sensitized with shrimp extract in combination with cholera toxin as adjuvant may be a suitable model to study shrimp allergy.

Reactivity of Shrimp Allergy-Related IgE Antibodies to Krill Tropomyosin

“…Recombinant allergens are considered the basis for new diagnostic approaches and development of novel strategies of allergen-specific immunotherapy, and recombinant tropomyosins have often been produced as fusion proteins in E. coli [6, 7, 10, 12, 14, 25]. Although the characteristics of fused recombinant tropomyosins have been similar to those of the original tropomyosins [6, 7, 12], for the development of novel strategies of crustacean allergic-specific immunotherapy it would be preferable if they were produced as a nonfusion protein rather than any fusion protein.…”

“…Therefore, tropomyosin in invertebrates is thought to be a panallergen [3, 5]. Shrimp tropomyosins have been well documented among crustacean allergens [3, 5, 7, 13, 14], and the shrimp-specific IgE-binding regions in the brown shrimp Pen a 1 (tropomyosin of Penaeus aztecus ) have also been identified using synthetic peptides and sera of 18 shrimp-allergic patients [12, 15, 16]. …”

“…Crustacean allergy does not appear to remit easily, and the allergy reaction causes itching, hives, swelling of the lips and tongue, pulmonary symptoms, gastrointestinal symptoms and anaphylactic shock [1,2,3]. The major crustacean allergen, a heat-stable 34- to 38-kDa protein, has been reported to be tropomyosin which is associated with the thin filament in muscle and microfilaments in nonmuscle cells in all eukaryotic cells [3,4,5,6,7]. The tropomyosin in invertebrates is a highly conserved protein in amino acid sequence among a wide range of invertebrate animals and has been suggested to be a cross-reacting allergen; thus it is reported that some patients allergic to shrimp are allergic to other crustaceans and mollusks or nonedible insects [5, 6,8,9,10].…”

Molecular characterization of Der p 10: a diagnostic marker for broad sensitization in house dust mite allergy

“…Two μL aliquots of natural and recombinant HDM allergens (nDer p 1, rDer p 2, rDer p 5, rDer p 7, rDer p 10 and rDer p 21) [19][20][21][22] as well as BSA as a control protein (each 0.25 μg/μL) were dotted onto nitrocellulose membranes (Schleicher & Schuell). The membranes were blocked with gold buffer [50 mM sodium phosphate pH 7.4, 0.5% (v/v) Tween-20, 0.5% (w/v) BSA and 0.05% (w/v) sodium azide], twice for 5 min and once for 30 min, and incubated with mite-allergic patients' sera and, for control purposes, with serum from a nonallergic individual, diluted 1 : 10 in gold buffer o/n at 4 °C.…”

Contribution of Structural Reversibility to the Heat Stability of the Tropomyosin Shrimp Allergen

“…Tropomyosin generally has anhelical structure 11) and forms dimers in muscle fiber. 10) -Helical structures are easily denatured by heat, and this is one of the principal causes of the denaturation and aggregation of proteins with intermolecular disulfide bonds.…”