Differences in titres of IgE, IgG4 and other IgG subclass anti‐ Der p 2 antibodies in allergic and non‐allergic patients measured with recombinant allergen

Tame, Atsushi; Sakiyama, Yukio; Kobayashi, Ichiro; Terai, Itaru; Kobayashi, Kunihiko

doi:10.1111/j.1365-2222.1996.tb00055.x

Cited by 26 publications

(23 citation statements)

References 24 publications

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“…In contrast to the group 1 allergens, the group 2 proteins have been easy to produce as recombinant allergens in E. coli in fused [181, 182]and unfused forms [113, 183], although the latter must be renatured. Der p 2 can be secreted from S. cerevisiae in a form essentially indistinguishable from the natural allergen [184].…”

Section: Recombinant Mite Allergensmentioning

confidence: 99%

Characterization and Immunobiology of House Dust Mite Allergens

Thomas¹,

Smith²,

Hales³

et al. 2002

Int Arch Allergy Immunol

304

254

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The examination of house dust mite extracts has indicated that over 30 different proteins can induce IgE antibody in patients allergic to the house dust mite. There are however dominant specificities especially the group 1 and 2 allergens which can account for much of the allergenicity of extracts. Of the 19 denominated allergens, the major IgE binding has been reported for the group 1, 2, 3, 9, 11, 14 and 15 allergens. The high-molecular-weight group 11, 14 and 15 allergens have only recently been described and although high IgE binding has been anticipated from immunoblotting, there is a need for considerable corroboration. Similarly, the study of the group 3 and 9 serine protease allergens has been incomplete. The group 4, 5, 7 and 8 allergens have shown intermediate IgE binding and the group 10 tropomyosins are of interest because of their potential cross-reactivity with allergen from disparate species. Although the progress with the production of recombinant group 1 allergens has been recent, many of the allergens can be produced as high IgE-binding polypeptides. The tertiary structure of the group 2 allergens has been determined from recombinant proteins and they are an excellent model for the investigation of modified allergens. An unexpected property of the group 1, 2 and 3 allergens has been the high degree of polymorphism found by cDNA analysis. It has however been possible to identify sequences to represent the variation in the natural allergens. The group 7 and 14 allergens show secondary modifications which vary in different extracts creating batch variation. While some estimate of the importance of allergens can be obtained from IgE binding, few analyses of T-cell responses have been made and these regulate both the development of, and the protection from sensitization.

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Section: Recombinant Mite Allergensmentioning

confidence: 99%

Characterization and Immunobiology of House Dust Mite Allergens

Thomas¹,

Smith²,

Hales³

et al. 2002

Int Arch Allergy Immunol

304

254

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“…While previous studies on the role of allergenspecific IgG antibody responses were hampered by the lack of well-defined allergen preparations, purified recombinant allergens have now become available for measurements with defined components. Studies performed with recombinant Bet v 1 (23,24), the major birch pollen allergen, recombinant timothy grass-pollen allergens (Phi p 1, Phi p 2, and Phi p 5) (76), and recombinant Der f 2 (77,78) established the following points: 1) sera from allergic and nonallergic subjects contained allergen-specific IgG antibodies belonging to different subclasses 2) levels of allergen-specific IgE are poorly correlated with IgG subclass responses 3) with epitopes prepared from major allergens by recombinant DNA technology, it could be shown that IgE and IgG antibodies of allergic patients bind to the same and also different epitopes (78).…”

Section: Ige-binding Haptens From Major Allergens and Allergen-specifmentioning

confidence: 99%

Recombinant allergens

Valenta

Vrtala

Laffer

et al. 1998

Allergy

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A great variety of recombinant plant, mite, mold, mammal, and insect allergens have been expressed in heterologous hosts (e.g., Escherichia coli), their cDNA being used as a template. The number of biologically active recombinant allergens available for experimental, diagnostic, and therapeutic purposes is increasing tremendously. Recombinant allergens have proven to be valuable tools to investigate T‐cell and B‐cell recognition of allergens as well as to study mechanisms of specific IgE regulation. The immunologic equivalence of many relevant recombinant allergens with their natural counterparts has been demonstrated, and the three‐dimensional structures of several recombinant allergens have been described recently. As a result of extensive cross‐reactivities among the relevant allergens, it appears that the number of epitopes needed for diagnosis and specific immunotherapy is less diverse than originally anticipated and might be soon covered by recombinant molecules. Recombinant allergens have been used for successful in vitro, as well as in vivo, allergy diagnosis, and work is in progress to produce recombinant allergen derivatives with reduced anaphylactic potential to improve current forms of immunotherapy.

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“…Such findings have also been reported with L. destructor allergen extract [27]. Others have reported similar IgG1 levels to rDer p 2 in children regardless of atopic status [23, 25]. Although the levels were lower in children with a documented low exposure to Dermatophagoides there was still no atopy-related difference [23].…”

Section: Discussionmentioning

confidence: 47%

“…It is considered that immunotherapy gives a rise in mainly the IgG1 and IgG4 subclasses and that the magnitude, the ratio or kinetic appearance between the two isotypes may predict the outcome of treatment [5, 22]. The few studies on natural exposures suggest a similar pattern [23, 24]or perhaps more IgG4-restricted response to aeroallergen extracts among atopics as compared to nonatopics [25, 26, 27, 28]. Our data with recombinant Lep d 2(wt) are in agreement with the latter studies and the levels of IgG4 and IgE clearly correlated as previously reported in some studies [28]but not others [25].…”

Section: Discussionmentioning

confidence: 98%

“…The few studies on natural exposures suggest a similar pattern [23, 24]or perhaps more IgG4-restricted response to aeroallergen extracts among atopics as compared to nonatopics [25, 26, 27, 28]. Our data with recombinant Lep d 2(wt) are in agreement with the latter studies and the levels of IgG4 and IgE clearly correlated as previously reported in some studies [28]but not others [25]. It is noteworthy that among the farmers it is only those sensitized to L. destructor who develop IgG4 Ab despite an expected similar level of exposure to dust mite allergen among all farmers [2].…”

Section: Discussionmentioning

confidence: 99%

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IgG1, IgG4 and IgE Antibody Reactivity to Mutant Forms of the Major Dust Mite Allergen Lep d 2 among Atopic and Nonatopic Subjects Naturally Exposed to <i>Lepidoglyphus destructor</i>

Olsson

Hage

Magnusson

2001

Int Arch Allergy Immunol

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Background: Lepidoglyphus destructor is a common dust mite causing IgE-mediated sensitization. The major allergen, Lep d 2, has previously been cloned and expressed as several double Cys to Ser mutants with the purpose of producing hypoallergenic variants for immunotherapy. Our aim was to investigate the reactivity pattern of IgG1, IgG4 and IgE antibodies to wild-type (wt) rLep d 2 and four mutants among atopic and nonatopic subjects in relation to sensitization and exposure to L. destructor. Methods: Inhibition and sandwich ELISA were used to compare IgG1, IgG4 and IgE antibody reactivities to rLep d 2 variants in serum of 20 atopic and 18 nonatopic farmers naturally exposed to L. destructor. A group of 22 urban subjects served as controls. Results: Atopic farmers demonstrated correlating IgE and IgG4 levels to rLep d 2(wt) (r_s = 0.70; p < 0.0001) which were significantly (p < 0.0001) higher than those of nonatopic farmers and urban controls. No IgG4 antibodies were detected in nonatopic farmers despite chronic allergen exposure. A parallel reactivity pattern of IgE and IgG4 to all rLep d 2 mutants was observed. The mutant lacking all 3 disulfide bonds, rLep d 2.6Cys, demonstrated neither any IgE nor IgG4 reactivity. In contrast, IgG1 antibodies had a different reactivity pattern and were detected among most subjects irrespective of atopy, exposure to L. destructor or disulfide impairments in rLep d 2. Moreover, IgG1 levels to rLep d 2(wt) and rLep d 2.6Cys correlated (n = 60; r_s = 0.65; p < 0.0001). Conclusions: IgE/IgG4 Ab to rLep d 2 were restricted to atopic farmers and demonstrated parallel recognition patterns of conformational epitopes. In contrast, IgG1 antibodies are ubiquitously found and mainly recognize sequential structures. The observed isotypic difference and interindividual variation in antibody specificities among atopic and nonatopic subjects imply careful investigation of hypoallergenic variants destined for immunotherapy.

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Differences in titres of IgE, IgG4 and other IgG subclass anti‐ Der p 2 antibodies in allergic and non‐allergic patients measured with recombinant allergen

Abstract: Results indicate that the induction of Der p 2-specific IgG4 in allergic diseases is independent to IgE as well as other IgG subclasses.

Cited by 26 publications

References 24 publications

Characterization and Immunobiology of House Dust Mite Allergens

Characterization and Immunobiology of House Dust Mite Allergens

Recombinant allergens

IgG1, IgG4 and IgE Antibody Reactivity to Mutant Forms of the Major Dust Mite Allergen Lep d 2 among Atopic and Nonatopic Subjects Naturally Exposed to <i>Lepidoglyphus destructor</i>

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