Allergenicity of Recombinant Troponin C from &lt;i&gt;Tyrophagus putrescentiae&lt;/i&gt;

Jeong, Kyoung Yong; Kim, Chung Ryul; Un, Sunjin; Yi, Myung Hee; Lee, In Yong; Park, Jung Won; Hong, Chein Soo; Yong, Tai Soon

doi:10.1159/000242358

Cited by 21 publications

(15 citation statements)

References 46 publications

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“…This suggests that minor allergens play an important role in some cases. For troponin C, Tyr p 24, a 10.6% IgE binding frequency was detected, but it did not significantly inhibit IgE reactivity to crude extract 117. The frequency of IgE reactivity to recombinant α-tubulin from T. putrescentiae was 29.3%, although its titer was very low 140.…”

Section: Hdm Allergen: Relevant Allergenic Components In Korean Patientsmentioning

confidence: 89%

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House Dust Mite Allergy in Korea: The Most Important Inhalant Allergen in Current and Future

Jeong

Park

Hong

2012

Allergy Asthma Immunol Res

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The house-dust mite (HDM), commonly found in human dwellings, is an important source of inhalant and contact allergens. In this report, the importance of HDM allergy in Korea and the characteristics of allergens from dust mite are reviewed with an emphasis on investigations performed in Korea. In Korea, Dermatophagoides farinae is the dominant species of HDM, followed by D. pteronyssinus. Tyrophagus putrescentiae is also found in Korea, but its role in respiratory allergic disease in Korea is controversial. The relatively low densities of mite populations and concentrations of mite major allergens in dust samples from Korean homes, compared to westernized countries, are thought to reflect not only different climatic conditions, but also cultural differences, such as the use of 'ondol' under-floor heating systems in Korean houses. HDM are found in more than 90% of Korean houses, and the level of exposure to HDM is clinically significant. About 40%-60% of Korean patients suffering from respiratory allergies, and more than 40% of patients suffering from atopic dermatitis, are sensitized to HDM. Mite allergens can be summarized according to their inherent auto-adjuvant activities and/or their binding affinities to the adjuvant-like substances: proteolytic enzymes, lipid binding proteins, chitin binding proteins, and allergens not associated with adjuvant-like activity. In general, allergens with a strong adjuvant-like activity or adjuvant-binding activity elicit potent IgE reactivity. In Korea, Der f 2 is the most potent allergen, followed by Der f 1. Immune responses are modulated by the properties of the allergen itself and by the adjuvant-like substances that are concomitantly administered with the antigens. Characterization of allergenic molecules and elucidation of mechanisms by which adjuvant-like molecules modulate allergic reactions, not only in Korea but also worldwide, will provide valuable information on allergic diseases, and are necessary for the development of diagnostic tools and therapeutic strategies.

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Section: Hdm Allergen: Relevant Allergenic Components In Korean Patientsmentioning

confidence: 89%

“…Troponin C, a mite group 24 allergen, was recently described as an allergen from T. putrescentiae 117. Interestingly, the IgE reactivity of Tyr p 24 was dependent on the Ca 2+ concentration.…”

Section: Hdm Allergen: Relevant Allergenic Components In Korean Patientsmentioning

confidence: 99%

House Dust Mite Allergy in Korea: The Most Important Inhalant Allergen in Current and Future

Jeong

Park

Hong

2012

Allergy Asthma Immunol Res

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“…In a recent study by Pascal et al , sensitization to TpC was found in 17.2% of 58 shrimp‐allergic patients. TpC has also been identified in cockroach and storage mites ( Tyrophagus putrescentiae ) .…”

Section: Allergensmentioning

confidence: 99%

Shellfish allergens: tropomyosin and beyond

Faber

Pascal

Kharbouchi

et al. 2017

Allergy

132

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IgE-mediated shellfish allergy constitutes an important cause of food-related adverse reactions. Shellfish are classified into mollusks and crustaceans, the latter belonging to the class of arthropoda. Among crustaceans, shrimps are the most predominant cause of allergic reactions and thus more extensively studied. Several major and minor allergens have been identified and cloned. Among them, invertebrate tropomyosin, arginine kinase, myosin light chain, sarcoplasmic calciumbinding protein, and hemocyanin are the most relevant. This review summarizes our current knowledge about these allergens.IgE-mediated shellfish allergy constitutes an important and increasing health issue in both children and adults (1, 2). During the last two decades, significant progress in biochemistry and molecular biology enabled the characterization, cloning, and recombinant production of various shellfish allergen components and epitope-emulating peptides that might become available for quantification of specific IgE (sIgE) antibodies, namely molecular diagnosis. This review intends to summarize our current knowledge about shellfish allergens and their cross-reactivity as this might be the key to optimize diagnosis (3, 4). Table 1 summarizes the most relevant shellfish allergens that have currently been characterized. Tropomyosin is considered to be the major allergen in shellfish allergy. Actually, already in the early 1980s Hoffman et al. (5) identified a heat-stable IgE-binding allergen in shrimps that was later identified as tropomyosin in brown shrimp (Penaeus aztecus) reacting with 28/ 34 (82%) of shrimp-sensitive individuals (6). Moreover, tropomyosin has been identified as a panallergen of many invertebrate species including other crustaceans (lobster, crab), mollusks (mussels, oysters, scallops, octopus, squids, snails, abalones, whelk, clams, razor shell), cockroaches, and mites (7-18). Tropomyosins are present in both muscle and nonmuscle cells. In striated muscle, they mediate the interaction of troponin-actin complex to regulate contraction. Note that tropomyosins from crustaceans share a high homology (up to 98%), whereas the amino acid sequence identity between (3,(19)(20)(21)(22)(23)(24)(25). Children were once reported to recognize a greater epitope repertoire than adults and thus suggested that shrimp sensitization could decrease over age (22). However, more recent studies with challenged patients could not reproduce this observation with the same epitope mapping (3, 24). About one decade ago, a recombinant tropomyosin from Penaeus aztecus, rPen a 1, became commercially available for molecular diagnostic testing, with improved results as a diagnostic tool in comparison with the whole-shrimp extract (26,27). In addition to tropomyosin, several other allergenic components have been identified in shellfish. In 2003, Yu et al. identified a novel allergen in Penaeus monodon (black tiger shrimp) (28), designated as Pen m 2, with arginine kinase activity. Similar to tropomyosin, arginine kinase is highly abundant i...

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“…Tyrophagus putrescentiae is one of the predominant SM species in Korea. Five Tyrophagus putrescentiae allergens have been described to date: Tyr p 2, Tyr p 3, Tyr p 8, Tyr p 10 and Tyr p 24 (16). Of these, Tyr p 2, Tyr p 8 and Tyr p 10 have been shown to cause cross-reactivity (6,11,15,17).…”

Section: Introductionmentioning

confidence: 99%

Cross-reactivity between group-5 and -21 mite allergens from Dermatophagoides farinae, Tyrophagus putrescentiae and Blomia tropicalis

Kim

Jeong

et al. 2015

Molecular Medicine Reports

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Abstract. Group-5 and group-21 allergens, produced by house dust mites and storage mites are 36.6-55.8% identical in their sequences and are recognized by at least 50% of immunoglobulin (Ig)E from the sera of individuals allergic to dust mites. In the present study, recombinant group-5 and -21 allergens from three mite species, Dermatophagoides farinae (rDer f 5 and 21), Tyrophagus putrescentiae (rTyr p 5 and 21), and Blomia tropicalis (rBlo t 5 and 21), were purified from Escherichia coli, and the IgE reactivities and cross-reactivities of these allergen variants were assessed. The IgE binding frequencies of rDer f 5, rDer f 21, rTyr p 5, rTyr p 21, rBlo t and rBlo t 21 proteins were 64. 95, 65.98, 30.41, 41.24, 30.93 and 21.65%, respectively. The IgE reactivity of rDer f 5 correlated highly with that of rDer f 21 (r=0.733). rTyr p 5 exhibited the highest level of correlation with rTyr p 21 (r=0.950), while the correlation of rBlo t 5 with rBlo t 21 was the lowest observed (r=0.104). The binding of IgE to rDer f 5 and rDer f 21 was not inhibited by any allergens but themselves. While rDer f 5 inhibited only 60.3% of IgE binding to rBlo t 5, rDer f 21 exhibited a high inhibitory effect against rTyr p 5 (93.01%), rTyr p 21 (92.12%), rBlo t 5 (86.97%) and rBlo t 21 (70.30%), implying cross-reactivity among mite species. The results of the present study demonstrated that the majority of the IgE reactivity to group-5 and -21 storage mite allergens is due to cross-reaction. It is therefore imperative to develop an accurate, component-resolved diagnosis for dust mite allergies.

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Allergenicity of Recombinant Troponin C from <i>Tyrophagus putrescentiae</i>

Cited by 21 publications

References 46 publications

House Dust Mite Allergy in Korea: The Most Important Inhalant Allergen in Current and Future

House Dust Mite Allergy in Korea: The Most Important Inhalant Allergen in Current and Future

Shellfish allergens: tropomyosin and beyond

Cross-reactivity between group-5 and -21 mite allergens from Dermatophagoides farinae, Tyrophagus putrescentiae and Blomia tropicalis

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