Immunoglobulin E Reactivity of Recombinant Allergen Tyr p 13 from
 Tyrophagus putrescentiae
 Homologous to Fatty Acid Binding Protein

Jeong, Kyoung Yong; Kim, Woo Kyung; Lee, Jae Sik; Lee, Jong Weon; Lee, In Yong; Kim, Kyu Earn; Hong, Chein Soo; Ree, Han-Il; Yong, Tai Soon

doi:10.1128/cdli.12.5.581-585.2005

Cited by 23 publications

(14 citation statements)

References 26 publications

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“…However, neither allergen significantly inhibited IgE binding to crude extracts. Recombinant fatty acid-binding protein, Tyr p 13, was recognized in 6.4% of sera from T. putrescentiae -sensitized subjects 92. Recombinant Tyr p 13 was able to inhibit up to 61.9% of IgE reactivity to crude extract in serum.…”

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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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: 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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“…To express the recombinant troponin C from T. putrescentiate , we PCR-amplified the open reading frame using primers (forward, 5′- GGATCC TATGTCGGTCGAACTATC-3′; reverse, 5′- CTCGAG TTAATCACCAGTCATCAT-3′) using the plasmid-containing troponin C sequence, which was obtained by the analysis of expressed sequence tags of T. putrescentiae [7], as template. The underlined sequences indicate the Bam HI and Xho I restriction sites, which were incorporated for directional cloning.…”

Section: Methodsmentioning

confidence: 99%

“…Five IgE-reactive proteins have been identified from T. putrescentiae , including Tyr p 2 [4], Tyr p 3 [5], Tyr p 10 [6], Tyr p 13 [7] and α-tubulin [8]. …”

Section: Introductionmentioning

confidence: 99%

Allergenicity of Recombinant Troponin C from Tyrophagus putrescentiae

Jeong¹,

Kim²,

Un³

et al. 2009

Int Arch Allergy Immunol

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Background: The storage mite, Tyrophagus putrescentiae, produces potent allergens, many of which have not been characterized. This study was undertaken to characterize the allergenicity of troponin C from T. putrescentiae.Methods: A cDNA encoding 17.7 kDa troponin C, with homology to cockroach allergen Bla g 6, was identified from T. putrescentiae-expressed sequence tags. Recombinant troponin C was expressed and IgE responses to the recombinant protein were assessed in the presence and absence of 10 mM CaCl₂. Cross-reactivity between T. putrescentiae troponin C and Bla g 6 was tested using an inhibition ELISA. Results: Recombinant T. putrescentiae troponin C shares 62.7–85.5% homology with troponin C from various arthropods. Sera from 5 of 47 subjects in our study group (10.6%) showed IgE binding to the recombinant protein. Interestingly, addition of 10 mM CaCl₂ increased the intensity of IgE binding approximately 2-fold. In an immune-inhibition ELISA with these sera, T. putrescetiae troponin C and Bla g 6 did not cross-react significantly. Conclusions: Troponin C is a new mite allergen with calcium-dependent IgE reactivity.

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“…At least 20 IgE-binding allergenic components of T. putrescentiae have been distinguished previously [1]. So far, only four allergens with full-length sequences of T. putrescentiae have been characterized and published: Tyr p 2 [11], Tyr p 10 (tropomyosin) [12], Tyr p 13 (fatty acid-binding protein) [13] and Tyr p α (tubulin) [14]. However, many allergenic components of T. putrescentiae have not been clarified to date, especially those with protease activity.…”

Section: Introductionmentioning

confidence: 99%

Immunologic Characterization and Allergenicity of Recombinant Tyr p 3 Allergen from the Storage Mite Tyrophagus putrescentiae

Liao¹,

Hsu²,

Tsai³

et al. 2009

Int Arch Allergy Immunol

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Background: The involvement of the storage mite Tyrophagus putrescentiae in allergies has been increasingly reported in many countries. Molecular analysis has shown that group 3 mite allergens are homologous to trypsin. Similar allergens have not been identified in T. putrescentiae. Our aims were to characterize group 3 allergens in T. putrescentiae and to investigate their significance in allergenicity. Methods: cDNAs of PreTyr p 3 and rTyr p 3 from T. putrescentiae were cloned and expressed in Escherichia coli. Native Tyr p 3 (nTyr p 3) was purified from spent growth medium with an affinity column coupling of antibody. Biological activities of rTyr p 3 were compared with nTyr p 3 in terms of IgE activity, enzymatic activity and histamine release. Results: Full-length cDNA of PreTyr p 3 encodes a 285-amino acid trypsin-like protease and acquires enzymatic activity after removing the pre- and pro-sequences. rTyr p 3 is a 26-kDa protein with equivalent IgE reactivity but weaker enzymatic activity than that of nTyr p 3. A limited level of cross-reactivity has been found between rTyr p 3, Der p 3 and Blomia. Eight of 10 T. putrescentiae-sensitized individuals showed >50% histamine release after triggering with rTyr p 3. Conclusions: Our studies demonstrate that Tyr p 3 is a frequent allergen (58%) in T. putrescentiae-sensitized patients. Since rTyr p 3 displays equivalent biological activities as nTyr p 3, the role of group 3 allergens can be studied using rTyr p 3 to elucidate the pathogenic effects and diagnostic applications of Tyr p 3.

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Immunoglobulin E Reactivity of Recombinant Allergen Tyr p 13 from Tyrophagus putrescentiae Homologous to Fatty Acid Binding Protein

Cited by 23 publications

References 26 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

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

Immunologic Characterization and Allergenicity of Recombinant Tyr p 3 Allergen from the Storage Mite <i>Tyrophagus putrescentiae</i>

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