Periplaneta americana Arginine Kinase as a Major Cockroach Allergen among Thai Patients with Major Cockroach Allergies

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Background: Cockroach (CR) allergens frequently cause severe asthma in CR-sensitized subjects. Allergen-specific immunotherapy causes a shift of allergic Th2 responses towards Th1 and/or regulatory T cell (Treg) responses which reduce airway inflammation and prevent disease progression. Data are relatively limited on immunotherapy via CR allergy vaccine. Methods: The therapeutic efficacy of an intranasal liposome-adjuvant vaccine made of a refined Periplaneta americana arginine kinase (AK) was compared to the liposome-entrapped P. americana crude extract (CRE) vaccine. Adult BALB/c mice were rendered allergic to CRE. Three allergic mouse groups were immunized intranasally on alternate days with 8 doses of liposome-entrapped CRE (L-CRE), liposome-entrapped AK and placebo, respectively. One week later, all mice received a nebulized CRE provocation. Evaluation of vaccine efficacy was performed 1 day after provocation. Results: Liposome-entrapped native AK attenuated airway inflammation after the CRE provocation and caused a shift of allergic Th2 to Th1 and Treg responses. The L-CRE also induced a shift from the Th2 to the Th1 response but did not induce a Treg response and could not attenuate the airway inflammation upon allergen reexposure. Conclusions: Intranasal liposome-adjuvant CR allergy vaccine containing native AK (Per a 9) is better than L-CRE in attenuating allergic airway inflammation. The findings of this study not only document a more comprehensive and beneficial immune response induced by the refined allergen vaccine but also raise the point that the shift from the Th2 to the Th1 response alone might not correlate with improved airway histopathology, clinical outcome and quality of life.

Section: Introductionmentioning

confidence: 99%

Intranasal, Liposome-Adjuvanted Cockroach Allergy Vaccines Made of Refined Major Allergen and Whole-Body Extract of Periplaneta americana

Meechan¹,

Tungtrongchitr

Chaisri

et al. 2013

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“…Several AKs have recently been characterized as allergens [9,10,11,12], and subsequently have been proposed to be a type of panallergen [12]. Therefore, sera from 10 skin prick test (SPT)-positive patients reactive to silkworm crude extract (SCE) were tested for their reactivity to AK from B. mori ( Bm AK).…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of an Arginine Kinase as a Major Allergen from Silkworm (Bombyx mori) Larvae

Liu

Xia

Yu-lan

et al. 2009

101

Background: The silkworm, Bombyx mori, is an important insect in the textile industry and its pupa are used in Chinese cuisine and traditional Chinese medicine. The silk, urine and dander of silkworms is often the cause of allergies in sericulture workers and the pupa has been found to be a food allergen in China. Recent studies have focused on reporting cases of silkworm allergies, but only a few studies have addressed the specific allergens present in the B. mori silkworm. Methods: We collected sera from 10 patients with a positive skin prick test to silkworm crude extract (SCE) and analyzed these samples by Western blot and ELISA. The cDNA of arginine kinase from the B. mori silkworm was also cloned and expressed in high yield in Escherichia coli. Allergenicity and cross-allergenicity of the recombinant B. mori arginine kinase (rBmAK) were investigated by ELISA inhibition assay. Results: Collected sera all reacted to a 42-kDa protein in a Western blot with SCE as the antigen. Preincubation of sera with rBmAK eliminated the reactivity of the patients’ sera to this 42-kDa band. All patient sera also exhibited positive reactivity to SCE in an ELISA assay. BmAK also demonstrated cross-reactivity with a recombinant AK from cockroach. Conclusion: Arginine kinase from the B. mori silkworm is a major allergen and crossreacts with cockroach AK.

“…It has also been demonstrated that shrimp AK caused allergic reaction in hypersensitive individuals [12]. AK is a panallergen in other invertebrates such as the moth [1], cockroach [13] and lobster [14]. …”

Section: Introductionmentioning

confidence: 99%

Molecular Characterization of Arginine Kinase, an Allergen from the Shrimp Litopenaeus vannamei

García-Orozco

Aispuro‐Hernández

Yépiz-Plascencia

et al. 2007

149

Background: Consumption of seafood can produce allergic symptoms in susceptible individuals and crustacean allergies are the most frequently reported causes of allergic reactions. Methods: An allergen from the muscle of the white shrimp Litopenaeus vannamei was purified by ion exchange chromatography and identified by mass spectrometry of tryptic peptides and its specific enzymatic activity. Moreover, the corresponding full-length cDNA was obtained from an L. vannamei muscle cDNA library. Results: A 40-kDa protein was purified and identified as arginine kinase and its cDNA of 1.4 kb encoded a 356 amino acid protein. The obtained arginine kinase was recognized by IgE in serum from shrimp-allergic individuals using ELISA and immunoblotting analysis. Conclusions: This is the first allergen reported for the Pacific white shrimp species; it was named Lit v 2 and has a 96% identity to Pen m 2 from Penaeus monodon.