Isolation and characterization of native Cry j 3 from Japanese cedar (Cryptomeria japonica) pollen

Fujimura, Takashi; Futamura, Norihiro; Midoro-Horiuti, Terumi; Togawa, Akihisa; Goldblum, Randall M.; Yasueda, Hiroshi; Saito, Akemi; Shinohara, Kenji; Masuda, Kenichi; Kurata, Kentaro; Sakaguchi, Masahiro

doi:10.1111/j.1398-9995.2007.01331.x

Cited by 42 publications

(22 citation statements)

References 36 publications

(42 reference statements)

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“…First, the booklice extract was coated on a polystyrene microtiter plate with 96 wells (1 µg dry weight/well), and diluted serum was preincubated with a serial dilution (1:10) of an inhibitor extract (from 0.1 µg/ml to 1 mg/ml) and applied to booklouse extract-coated wells. IgE reactivity in this inhibition analysis was measured by fluorometric ELISA as previously described [24]. The results were calculated as a percentage of inhibition.…”

Section: Methodsmentioning

confidence: 99%

Allergenicity and Cross-Reactivity of Booklice (Liposcelis bostrichophila): A Common Household Insect Pest in Japan

Fukutomi¹,

Kawakami²,

Taniguchi³

et al. 2011

Int Arch Allergy Immunol

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Background: Booklice (Liposcelis bostrichophila) are a common household insect pest distributed worldwide. Particularly in Japan, they infest ‘tatami’ mats and are the most frequently detected insect among all detectable insects, present at a frequency of about 90% in dust samples. Although it has been hypothesized that they are an important indoor allergen, studies on their allergenicity have been limited. Methods: To clarify the allergenicity of booklice and the cross-reactivity of this insect allergen with allergens of other insects, patients sensitized to booklice were identified from 185 Japanese adults with allergic asthma using skin tests and IgE-ELISA. IgE-inhibition analysis, immunoblotting and immunoblotting-inhibition analysis were performed using sera from these patients. Allergenic proteins contributing to specific sensitization to booklice were identified by two-dimensional electrophoresis and two-dimensional immunoblotting. Results: The booklouse-specific IgE antibody was detected in sera from 41 patients (22% of studied patients). IgE inhibition analysis revealed that IgE reactivity to the booklouse allergen in the sera from one third of booklouse-sensitized patients was not inhibited by preincubation with extracts from any other environmental insects in this study. Immunoblotting identified a 26-kD protein from booklouse extract as the allergenic protein contributing to specific sensitization to booklice. The amino acid sequence of peptide fragments of this protein showed no homology to those of previously described allergenic proteins, indicating that this protein is a new allergen. Conclusions: Sensitization to booklice was relatively common and specific sensitization to this insect not related to insect panallergy was indicated in this population.

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Section: Methodsmentioning

confidence: 99%

Allergenicity and Cross-Reactivity of Booklice (Liposcelis bostrichophila): A Common Household Insect Pest in Japan

Fukutomi¹,

Kawakami²,

Taniguchi³

et al. 2011

Int Arch Allergy Immunol

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“…Several members of the TLP family have been identified as major allergens in Cupressaceae pollen such as Jun a 3 [10], Cup a 3 [11], and Cry j 3 [12] as well as in plant foods such as cherry [13], apple [5], kiwi [14], banana [15], orange [16], grape [17] and bell pepper [[18], reviewed in [19]]. PR-5-like sequences were also discovered in nematodes and insects revealing an ancient multigene family [20].…”

Section: Introductionmentioning

confidence: 99%

Mal d 2, the Thaumatin-Like Allergen from Apple, Is Highly Resistant to Gastrointestinal Digestion and Thermal Processing

Smole

Bublin

Radauer

et al. 2008

Int Arch Allergy Immunol

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Background: The stability of food allergens to proteolysis and thermal denaturation contributes considerably to their allergenicity. Methods: Mal d 2, an allergenic thaumatin-like protein (TLP) from apple, was isolated and purified by anion exchange chromatography. Its IgE reactivity was tested by ELISA and immunoblotting using sera from apple allergic patients. The proteolytic stability of Mal d 2 was investigated using two in vitro digestion models. Effects of thermal treatment at different pH values on the secondary structure of the protein were recorded by circular dichroism. The level and IgE reactivity of Mal d 2 present in industrially prepared foods were assessed. Results: Purified Mal d 2 consisted of two isoforms. Both harbored carbohydrate moieties and bound serum IgE from apple allergic individuals. Mal d 2 showed remarkable stability to proteolysis and thermal treatments. The allergen remained intact after 2 h each of gastric and subsequent duodenal digestion retaining its full IgE-binding capacity. Mal d 2 was unfolded at neutral and acidic pH at 70°C. Refolding after cooling was only observed at acidic pH. Mal d 2 detected by an anti-TLP antibody in cloudy apple juice did not bind IgE of a serum pool of apple allergic patients. Conclusion: Our findings suggest that Mal d 2 maintains its structure in the gastrointestinal tract, a feature essential for sensitizing the mucosal immune system and provoking allergic reactions.

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“…Allergenic TLPs have also been described in pollen grains of the mountain cedar (Jun a 3; Juniperus ashei) [24], in Cupressus arizonica pollen (Cup a 3) [25], and recently in Japanese cedar (Cry j 3; Cryptomeria japonica) [26].…”

Section: Introductionmentioning

confidence: 98%

Quantification of the thaumatin‐like kiwi allergen by a monoclonal antibody‐based ELISA

Gavrović-Jankulović¹,

Spasic

Veličković

et al. 2008

Molecular Nutrition Food Res

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Thaumatin-like proteins (TLPs) have been established as a new family of fruit and pollen allergens. The aim of this study was to develop a two-site ELISA for the quantification of the thaumatin-like kiwi allergen (Act d 2) in kiwifruit extracts and kiwifruit-containing food products. Genomic DNA (gDNA) of Act d 2 was amplified and the deduced amino acid sequence was determined to obtain a primary structure. Act d 2 purified from kiwifruit extract by HPLC was identified by Edman degradation and MS. Balb/c mice were immunized with Act d 2 for the production of mAbs by hybridoma technology. The optimized ELISA measured Act d 2 concentrations ranging from 0.2 to 9.0 ng/mL, with intra- and interassay coefficients of variation of 3.65 and 10.44%, respectively. The developed ELISA is a useful method for the quantification of the thaumatin-like kiwi allergen in kiwifruit extracts as well as the allergen level in kiwifruit-containing food products. It may be a helpful analytical tool for the evaluation of the stability (integrity) of fruit allergen extracts for in vitro diagnosis.

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Isolation and characterization of native Cry j 3 from Japanese cedar (Cryptomeria japonica) pollen

Cited by 42 publications

References 36 publications

Allergenicity and Cross-Reactivity of Booklice <i>(Liposcelis bostrichophila)</i>: A Common Household Insect Pest in Japan

Allergenicity and Cross-Reactivity of Booklice <i>(Liposcelis bostrichophila)</i>: A Common Household Insect Pest in Japan

Mal d 2, the Thaumatin-Like Allergen from Apple, Is Highly Resistant to Gastrointestinal Digestion and Thermal Processing

Quantification of the thaumatin‐like kiwi allergen by a monoclonal antibody‐based ELISA

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