Specific Measurement of a Major Mite Allergen,Der fII, by an Enzyme-linked Immunosorbent Assay System Using Monoclonal Anti-DerII Antibodies

Akagawa, Midori; Mori, Toshio; Ando, Tomoyuki; Okudaira, Hirokazu

doi:10.1271/bbb.56.1725

Cited by 14 publications

(7 citation statements)

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“…Using monoclonal antibody 15E11 as the solidphase antibody and alkaline phosphatase labeled mAb 13A4 as the secondary (detection is better) antibody [19], the binding of recombinant D e r fll from clones 2 and II was Fig.7. Trypsin-sensitivity o f three Der / I I variants.…”

Section: Discussionmentioning

confidence: 99%

Effects of Amino Acid Variations in Recombinant Der f ll on Its Human IgE and Mouse IgG Recognition

Nishiyama

Yuuki

Usui

et al. 1994

Int Arch Allergy Immunol

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Amino acid sequencing of the major mite allergen Der f Il purified from mite body extract revealed that it is a mixture of at least two variants. Substitutions were found only at positions in which amino acid variations were predicted from the nucleotide sequences of three cloned cDNAs. When cDNAs corresponding to the three variants were expressed in Escherichia coli, Der f ll proteins were produced as inclusion bodies. Denaturation and renaturation with urea converted recombinant Der f ll into a protein with three intramolecular disulfíde bonds (Cys8-Cys119, Cys21-Cys27, and Cys73-Cys78), which were identical to those previously identified in native Der f ll. All the variants, including native Der f Il, were equally recognized by human IgE antibodies from 14 different sera of mite-allergic patients. These results suggested that recombinant Der f ll proteins assumed a conformation identical to that of the native Der f ll and that all the Der f ll variants acted as allergens. This result also suggested that IgE antibody binds to the region where there were no amino acid variations. The binding ability of the monoclonal antibody (mAb) 18G8 for the variant clones 1, 2, and 11 Der f ll was almost the same. However, mAb 15E11 bound to clone 1 Der f ll more efficiently than to clones 2 and 11, whereas mAb 13A4 recognized clone 2 Der f ll as the most preferable antigen. This suggested that these antibodies recognized the region of amino acid variations. The stability of Der f ll variants was analyzed by measuring their IgE antibody binding activity after heating, freezing, or acid treatment, and was analyzed by resistance to trypsin digestion. These analyses revealed that clone 2 Der f ll was the most stable among the Der f ll variants.

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Section: Discussionmentioning

confidence: 99%

Effects of Amino Acid Variations in Recombinant Der f ll on Its Human IgE and Mouse IgG Recognition

Nishiyama

Yuuki

Usui

et al. 1994

Int Arch Allergy Immunol

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“…Since Der f2 has been shown to sensitize over 80% of patients with house-dust mite allergy, rDer f2 should prove useful in the diagnosis and immunotherapy of allergic asthma and rhinitis caused by house-dust mites. It should also provide a basis for research into allergies and immunology.In the present study, with special reference to the therapeutic application of rDer f2, we established a murine allergic model by intranasal or intraperitoneal injection of rDer f2 to A/J mice, which are highly responsive to Der f2 [7]. We examined the effect of oral-hyposensitization therapy with rDer f2 against the immediate bronchoconstriction in the intranasally sensitized animals because their reaction after rDer f2 inhalation was more intense than that of intraperitoneally immunized mice.…”

mentioning

confidence: 99%

“…In the present study, with special reference to the therapeutic application of rDer f2, we established a murine allergic model by intranasal or intraperitoneal injection of rDer f2 to A/J mice, which are highly responsive to Der f2 [7]. We examined the effect of oral-hyposensitization therapy with rDer f2 against the immediate bronchoconstriction in the intranasally sensitized animals because their reaction after rDer f2 inhalation was more intense than that of intraperitoneally immunized mice.…”

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confidence: 99%

Effects of oral hyposensitization with recombinant Der f2 on immediate airway constriction in a murine allergic model

Yasue

Yokota²,

Yuasa³

et al. 1998

Eur Respir J

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Recombinant Der f2 (rDer f2) has recently been developed as a promising allergen for the diagnosis and immunotherapy of house-dust mite allergy, and studies in immunology. The aim of the present study was to evaluate whether oral administration of rDer f2 could suppress an immediate allergic reaction in mice sensitized with mite allergen. We developed a murine allergic model that showed bronchoconstriction after inhalation of rDer f2, and studied the effect of oral administration of rDer f2 on the reaction.Seven week old male A/J mice were intranasally immunized with rDer f2 12 times. Sensitized mice showed anti-rDer f2 immunoglobulin (Ig)E production and immediate airway constriction after inhalation of 10 mg·mL -1 of rDer f2, as determined by the Konzett-Rössler method. Immunized animals were divided into three groups, and fed phosphate-buffered saline (PBS), 0.1 mg·day -1 , or 1 mg·day -1 of rDer f2 for 4 weeks, respectively. Seven days after the last feeding, the mice were examined for their immediate response.Animals fed with 1 mg·day -1 rDer f2 showed significantly reduced bronchoconstriction after inhalation of both 2 mg·mL -1 and 10 mg·mL -1 of rDer f2 compared with PBS-fed mice. Similar results were obtained when we examined mice 10 weeks after the last feeding. Reactions in the 0.1 mg·day -1 rDer f2-fed group also tended to decrease in comparison with PBS-fed animals. Plasma anti-rDer f2 IgE, IgG1, IgG2a, and IgG2b levels were not changed by feeding with rDer f2.We conclude that recombinant Der f2 exhibits both sensitizing and hyposensitizing activities in mice. rDer f2 may be useful in immunotherapy and diagnosis of housedust mite allergy. Eur Respir J 1998; 11: 144-150 To date, several clinically important allergens such as Der 1 and Der 2 have been identified in crude mite extract [1][2][3][4]. Among others, the structural gene of Der f2, one of the major mite allergens found in Dermatophagoides farinae was cloned, and the product (recombinant Der f2 (rDer f2)) shown to exhibit allergic activity in humans comparable with native Der f2 prepared from crude mite extract [5,6]. Since Der f2 has been shown to sensitize over 80% of patients with house-dust mite allergy, rDer f2 should prove useful in the diagnosis and immunotherapy of allergic asthma and rhinitis caused by house-dust mites. It should also provide a basis for research into allergies and immunology.In the present study, with special reference to the therapeutic application of rDer f2, we established a murine allergic model by intranasal or intraperitoneal injection of rDer f2 to A/J mice, which are highly responsive to Der f2 [7]. We examined the effect of oral-hyposensitization therapy with rDer f2 against the immediate bronchoconstriction in the intranasally sensitized animals because their reaction after rDer f2 inhalation was more intense than that of intraperitoneally immunized mice. Materials and methodsAntigen rDer f2, clone 1 [5], was kindly supplied by the Nikka Whisky Distilling Co., Ltd. (Chiba, Japan), and dissolved in...

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“…Although there have been some previous assays for measuring the Der 2 allergens, they measured both Der p 2 and Der f 2 as "Der 2' tising crossreacfive antibodies [12.14.15], or a single allergen. Der p 2 [18] or Der f 2 [19]. The Der 2 assay using crossreactive antibodies has the advantage that it can tneasure Der p 2 and Der f 2 in a single assay.…”

Section: Discussionmentioning

confidence: 99%

Species‐specific measurement of the second group of Dermatophagoides mite allergens, Der p 2 and Der f 2, using a monoclonal antibody‐based ELISA

Yasueda

Saito

Yanagihara

et al. 1996

Clin Experimental Allergy

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Specific Measurement of a Major Mite Allergen,Der fII, by an Enzyme-linked Immunosorbent Assay System Using Monoclonal Anti-DerII Antibodies

Cited by 14 publications

References 4 publications

Effects of Amino Acid Variations in Recombinant <i>Der f</i> ll on Its Human IgE and Mouse IgG Recognition

Effects of Amino Acid Variations in Recombinant <i>Der f</i> ll on Its Human IgE and Mouse IgG Recognition

Effects of oral hyposensitization with recombinant Der f2 on immediate airway constriction in a murine allergic model

Species‐specific measurement of the second group of Dermatophagoides mite allergens, Der p 2 and Der f 2, using a monoclonal antibody‐based ELISA

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