Cloning and characterization of a new allergen, Mag 3, from the house dust mite, Dermatophagoides farinae: Cross-reactivity with high-molecular-weight allergen

Fujikawa, Akihiro; Ishimaru, Noriyuki; Seto, A.; Yamada, Hiroyuki; Aki, Tsunehiro; Shigeta, Seiko; Wada, Takeshi; Jyo, Toshihiko; Murooka, Y; Oka, Satoru; Ono, Kazuhisa

doi:10.1016/0161-5890(95)00127-1

Cited by 32 publications

(41 citation statements)

References 32 publications

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“…The original reports described IgE binding by two peptide fragments, Mag 1 and Mag 3, which were expressed from partial cDNA clones [48, 49]. The binding to the whole allergen, isolated by antibodies to Mag 3, was similar in strength and frequency as the binding to Der f 2 [49].…”

Section: Ige Binding To Purified Allergensmentioning

confidence: 99%

“…The natural form of the allergen encountered in the environment may be complex and variable. The presence in extracts is known to be low, presumably due to stability because it is a very abundant protein in mite bodies [49]. …”

Section: Group 14 Allergensmentioning

confidence: 99%

“…The peptide, Mag 3, which was an arbitrary fragment expressed from a partial cDNA clone from D. farinae, was shown to be a part of a 177,000 MW allergen with the same strength of reactivity as Der f 1 and 2 in both IgE-binding and T-cell assays [49, 74]. The high-molecular-weight protein did not contain lipid or carbohydrate moieties and the staining of histological section showed it was distributed throughout the body [49]. Western blotting of extracts with anti-Mag 3 revealed many bands which varied with different extracts [13]although bands of over 70,000 MW were prominent.…”

Section: Group 14 Allergensmentioning

confidence: 99%

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Characterization and Immunobiology of House Dust Mite Allergens

Thomas¹,

Smith²,

Hales³

et al. 2002

Int Arch Allergy Immunol

303

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: Ige Binding To Purified Allergensmentioning

confidence: 99%

Section: Group 14 Allergensmentioning

confidence: 99%

Section: Group 14 Allergensmentioning

confidence: 99%

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Characterization and Immunobiology of House Dust Mite Allergens

Thomas¹,

Smith²,

Hales³

et al. 2002

Int Arch Allergy Immunol

303

254

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“…Thus far, the reported Bt allergens are low-molecular-weight proteins. Recent studies in other species of mites demonstrated the presence of high-molecular-weight allergens with significant IgE-binding properties from mite-sensitive patients [7, 12]. Der f 11 isolated from Dermatophagoides farinae is a 98-kD paramyosin allergen with a human IgE reactivity of 82% [13, 14]while Mag 3 (M-177) isolated from Dermatophagoides pteronyssinus is a 177-kD allergen with a human IgE reactivity of 70% [15].…”

Section: Introductionmentioning

confidence: 99%

cDNA Cloning and Expression of Blo t 11, the <i>Blomia tropicalis</i> Allergen Homologous to Paramyosin

Ramos¹,

Cheong

Lee³

et al. 2001

Int Arch Allergy Immunol

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Blomia tropicalis is an important mite species in many parts of the world and the most predominant mite species in tropical countries. The prevalence of sensitization to this species has probably been underestimated because commercial extracts are largely unavailable. Identification and characterization of B. tropicalis allergens is an important step toward understanding the role of this species in allergic sensitization and could provide appropriate reagents for diagnostic and therapeutic procedures. This paper describes the isolation, sequence analysis, expression and allergenicity of a cDNA gene coding for a B. tropicalis allergen with homology to paramyosin, a high-molecular-weight allergen previously identified in Dermatophagoides farinae. The full-length Blo t 11 cDNA gene was isolated by cDNA library screening, 5′-rapid amplification of cDNA ends and long-distance PCR. Sequence analysis was performed with a combination of CLUSTAL W, CGC and BLAST program packages. The cDNA gene was expressed as a GST fusion protein in Escherichia coli and purified by affinity chromatography using the glutathione Sepharose column. Allergenicity of the rBlo t 11 was tested by human IgE dot blot immunoassay. Blo t 11 is a 3,111-bp cDNA gene with a 2,625-bp open reading frame coding for an 875-amino acid protein, exhibiting significant homology with different invertebrate paramyosins. The human IgE dot blot immunoassay showed that the rBlo t 11 reacted positively to 52% (33/63) of sera from asthmatic patients. Blo t 11 is the homolog of Der f 11 exhibiting potentially important allergenic activity.

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“…Only Der f 1/2 and Der p 1/2 are used for the standardization of a vaccine for AIT of HDM. On the other hand, many allergens have been identified and characterized from HDM, including Dermatophagoides farinae (American HDM) and Dermatophagoides pteronyssinus (European HDM), as Der f/Der p allergens or mite allergen gene (Mag) allergens, such as Der f 6 and Mag3 (7)(8)(9)(10)(11)(12)(13)(14). Among the allergens, 28 from D. farinae have been formally registered in a database for systematic allergen nomenclature approved by the World Health Organization and the International Union of Immunological Societies (WHO/IUIS) Allergen Nomenclature Sub-committee.…”

mentioning

confidence: 99%

Der f 34, a Novel Major House Dust Mite Allergen Belonging to a Highly Conserved Rid/YjgF/YER057c/UK114 Family of Imine Deaminases

ElRamlawy

Fujimura

Baba

et al. 2016

Journal of Biological Chemistry

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The high prevalence of house dust mite (HDM) allergy is a growing health problem worldwide, and the characterization of clinically important HDM allergens is a prerequisite for the development of diagnostic and therapeutic strategies. Here, we report a novel HDM allergen that belongs structurally to the highly conserved Rid/YjgF/YER057c/UK114 family (Rid family) with imine deaminase activity. Isolated HDM cDNA, named der f 34, encodes 128 amino acids homologous to Rid-like proteins. This new protein belongs to the Rid family and has seven conserved residues involved in enamine/imine deaminase activity. Indeed, we demonstrated that purified Der f 34 had imine deaminase activity that preferentially acted on leucine and methionine. Native Der f 34 showed a high IgE binding frequency as revealed by two-dimensional immunoblotting (62.5%) or ELISA (68%), which was comparable with those of a major HDM allergen Der f 2 (77.5 and 79%, respectively). We also found that Der f 34 showed cross-reactivity with another prominent indoor allergen source, Aspergillus fumigatus. This is the first report showing that the Rid family imine deaminase represents an additional important pan-allergen that is conserved across organisms.Asthma is a serious global health problem that significantly reduces quality of life. In a cross-sectional World Health Organization survey of 178,215 individuals from 70 countries conducted in 2002-2003, it was estimated that 4.3% of adults (range, 0.2-21.0%) had been diagnosed with asthma by a medical doctor (1). Inhaled airborne allergens cause allergic inflammation via the cross-linking of allergen-specific IgEs bound on high affinity IgE receptor (FceRI) located on the surface of airway or lung mast cells, causing the secretion of inflammatory chemical mediators (e.g. histamine and leukotrienes) from activated mast cells. House dust mites (HDMs) 5 and fungi are major sources of airborne allergens and trigger asthmatic attacks in allergic patients concomitant with air pollutants (2).Allergen-specific immunotherapy (AIT) is the only curative treatment for allergic asthma that changes the natural course of an allergy (3). AIT induces allergen-specific tolerance by administering increasing doses of causative allergens subcutaneously or sublingually (4). The precise mechanisms underlying AIT remain to be fully elucidated, but the involvement of regulatory T cells and B cells or the induction of T cell anergy is suggested to be a key mechanism for an efficient AIT. AIT induces antigen-specific immunomodulatory cells or the anergic response of T cells specific to major allergens included in an allergen extract as an AIT vaccine. Therefore, the standardization of AIT vaccines using important major allergens and the characterization of major component allergens in an allergen source are important issues for the development of an effective AIT (5, 6).

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Cloning and characterization of a new allergen, Mag 3, from the house dust mite, Dermatophagoides farinae: Cross-reactivity with high-molecular-weight allergen

Cited by 32 publications

References 32 publications

Characterization and Immunobiology of House Dust Mite Allergens

Characterization and Immunobiology of House Dust Mite Allergens

cDNA Cloning and Expression of Blo t 11, the <i>Blomia tropicalis</i> Allergen Homologous to Paramyosin

Der f 34, a Novel Major House Dust Mite Allergen Belonging to a Highly Conserved Rid/YjgF/YER057c/UK114 Family of Imine Deaminases

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