Immunochemical characterization of recombinant and native tropomyosins as a new allergen from the house dust mite, Dermatophagoides farinae

Aki, Tsunehiro; Kodama, Takeshi; Fujikawa, Akihiro; Miura, Keisuke; Shigeta, Seiko; Wada, Takeshi; Jyo, Toshihiko; Murooka, Yoshikatsu; Oka, Satoru; Ono, Kazuhisa

doi:10.1016/s0091-6749(95)70035-8

Cited by 150 publications

(117 citation statements)

References 32 publications

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“…Three chitinase isoforms reported here have the similar molecular weight but different pI, which may be a result of varying amino acid sequences or glycosylation. Tropomyosin has been identified as Der f 10 in D. farinae (20).…”

Section: Analysis Of Dust Mite Allergen Components By 2-de and Igementioning

confidence: 99%

Dermatophagoides farinae Allergens Diversity Identification by Proteomics

Chen

Long

et al. 2013

Molecular & Cellular Proteomics

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The most important indoor allergens for humans are house dust mites (HDM). Fourteen Dermatophagoides farinae allergens (Der f 1-3, 6, 7, 10, 11, 13-18, and 22) are reported although more than 30 allergens have been estimated in D. farinae. Seventeen allergens belonging to 12 different groups were identified by a procedure of proteomics combined with two-dimensional immunoblotting from D. farina extracts. Their sequences were determined by Edman degradation, mass spectrometry analysis, and cDNA cloning. Their allergenicities were assayed by enzyme-linked immunosorbent assay inhibition tests, immunoblots, basophil activation test, and skin prick tests. Eight of them are the first report as D. farinae allergens. The procedure of using a proteomic approach combined with a purely discovery approach using sera of patients with broad IgE reactivity profiles to mite allergens was an effective method to investigate a more complete repertoire of D. farinae allergens. The identification of eight new D. farinae allergens will be helpful for HDM allergy diagnosis and therapy, especially for patients without response for HDM major allergens. In addition, the current work significantly extendedthe repertoire of D. farinae allergens. Molecular & Cellular

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Section: Analysis Of Dust Mite Allergen Components By 2-de and Igementioning

confidence: 99%

Dermatophagoides farinae Allergens Diversity Identification by Proteomics

Chen

Long

et al. 2013

Molecular & Cellular Proteomics

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“…Especially, IgE-binding frequencies of Mag3 and Mag44 were comparable to those of the major allergens [19,21]. Mag29 is nearly identical in sequence to heat shock protein (hsp) [20], while Mag44 has been identified as tropomyosin [21]. However, little information is available on the biological functions of the recombinant antigens.…”

Section: Introductionmentioning

confidence: 99%

Human T cell responses to recombinant mite antigens of Dermatophagoides farinae

Fujii

Ono

Shigeta

et al. 1997

Clinical and Experimental Immunology

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SUMMARYWe studied T cell responses to four glutathione S transferase (GST)-fused mite antigens prepared in our laboratory using peripheral blood lymphocytes from mite-sensitive patients with bronchial asthma. Of the four recombinant antigens, purified GST-Mag3 had the strongest ability to cause patients' lymphocytes to proliferate, and its potency was almost comparable to that of crude mite bodies (Dfb) and faeces (Dff) antigens and a purified major antigen, Der f 2. The responder lymphocytes were mainly T cells, because the proliferative response was depleted by the treatment of lymphocytes with anti-CD3 antibody and complement, but not with anti-CD20 antibody and complement. The responsiveness of lymphocytes to GST-Mag3 correlated with that to Der f 2, but GST-Mag3 displayed slightly higher activity to stimulate lymphocytes than Der f 2. Simultaneously, the levels of Dff-and GST-Mag3-specific IgE antibodies correlated with the responsiveness of lymphocytes to GST-Mag3. These results suggest that Mag3 is a new valuable antigen for the response of T cell proliferation in mite-sensitive patients.

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“…Pen a 1 inhibited at least 75% of patients' IgE radioallergosorbent test reactivity to whole body shrimp extract, indicating that Pen a 1 is also responsible for most of the allergenic activity of shrimp (2). Tropomyosin is a major allergen in other Crustacea species (3)(4)(5)(6) and in dust mite (7)(8)(9)(10)(11), cockroach (12,13), lobster (4), squid (14), and other mollusks (15)(16)(17)(18)(19), suggesting that tropomyosin may be regarded as an invertebrate pan-allergen (20). Indeed, cross-reactivity between cockroaches and mites with Crustacea was attributed to tropomyosin (4,21,22).…”

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confidence: 99%

Reduced Allergenic Potency of VR9-1, a Mutant of the Major Shrimp Allergen Pen a 1 (Tropomyosin)

Reese

Viebranz

Leong-Kee

et al. 2005

The Journal of Immunology

105

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The major shrimp allergen, tropomyosin, is an excellent model allergen for studying the influence of mutations within the primary structure on the allergenic potency of an allergen; Pen a 1 allows systematic evaluation and comparison of Ab-binding epitopes, because amino acid sequences of both allergenic and nonallergenic tropomyosins are known. Individually recognized IgE Ab-binding epitopes, amino acid positions, and substitutions critical for IgE Ab binding were identified by combinatorial substitution analysis, and 12 positions deemed critical were mutated in the eight major epitopes. The mutant VR9-1 was characterized with regard to allergenic potency by mediator release assays using sera from shrimp-allergic subjects and sera from BALB/c, C57BL/6J, C3H/HeJ, and CBA/J mice sensitized with shrimp extract using alum, cholera toxin, and Bordetella pertussis, as adjuvants. The secondary structure of VR9-1 was not altered; however, the allergenic potency was reduced by 90–98% measuring allergen-specific mediator release from humanized rat basophilic leukemia (RBL) cells, RBL 30/25. Reduced mediator release of RBL-2H3 cells sensitized with sera from mice that were immunized with shrimp extract indicated that mice produced IgE Abs to Pen a 1 and to the same epitopes as humans did. In conclusion, data obtained by mapping sequential epitopes were used to generate a Pen a 1 mutant with significantly reduced allergenic potency. Epitopes that are relevant for human IgE Ab binding are also major binding sites for murine IgE Abs. These results indicate that the murine model might be used to optimize the Pen a 1 mutant for future therapeutic use.

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Immunochemical characterization of recombinant and native tropomyosins as a new allergen from the house dust mite, Dermatophagoides farinae

Cited by 150 publications

References 32 publications

Dermatophagoides farinae Allergens Diversity Identification by Proteomics

Dermatophagoides farinae Allergens Diversity Identification by Proteomics

Human T cell responses to recombinant mite antigens of Dermatophagoides farinae

Reduced Allergenic Potency of VR9-1, a Mutant of the Major Shrimp Allergen Pen a 1 (Tropomyosin)

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