Isolation and characterization of a novel 98-kd Dermatophagoides farinae mite allergen

Tsai, Li-Ping; Chao, Pei-Ling; Shen, Horng-Der; Tang, Ren-Bin; Chang, Tsu-Chung; Chang, Zo-Nan; Hung, Mei-Whey; Lee, Bo-Liang; Chua, Kee Chaing

doi:10.1016/s0091-6749(98)70099-5

Cited by 61 publications

(73 citation statements)

References 35 publications

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“…2B and 3C, u). HDM group 11 allergen paramyosin has a molecular weight of 98 kDa, 19) but further analysis is necessary to determine whether the protein for the band is the HDM paramyosin. A major allergen of another nematode, Anisakis simplex, Ani s 2, is also paramyosin.…”

Section: Discussionmentioning

confidence: 99%

Immunization of Rabbits with NematodeAscaris lumbricoidesAntigens Induces Antibodies Cross-Reactive to House Dust MiteDermatophagoides farinaeAntigens

Nakazawa

Khan

Yasueda

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionmentioning

confidence: 99%

Immunization of Rabbits with NematodeAscaris lumbricoidesAntigens Induces Antibodies Cross-Reactive to House Dust MiteDermatophagoides farinaeAntigens

Nakazawa

Khan

Yasueda

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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“…The other four antigenic proteins with molecular masses of 76, 90, 98, and 170-kD had frequencies below 30%. Though the significance of these proteins of housedust mites in canine AD are not clear at present, high molecular weight proteins, 92, 98, 177-kD, were recently reported as one of the important allergens in the human athmatic patients [4,18]. They identified and characterized a 98-kD allergen against which greater than 80% of patients allergic to housedust mites showed IgE reactivity.…”

Section: Discussionmentioning

confidence: 99%

Determination of Antigenic Proteins of Housedust Mites in 90 Dogs Suffering from Atopic Dermatitis.

Yamashita

Fujiwara

R³

et al. 2002

The Journal of Veterinary Medical Science

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ABSTRACT. Housedust mites, Dermatophagoides pteronyssinus (D. pteronyssinus) and Dermatophagoides farinae (D. farinae), are the important causative agents of allergic diseases in human and animals. By using 165 dogs suffering from atopic dermatitis (AD), serum levels of immunogloblin E (IgE) antibody against 25 kinds of allergen including housedust mites were determined. Housedust mites were the most frequent allergen against which 90 of the 165 allergic dogs (54.5%) by IMMUNODOT assay. With the further analysis of immunoblotting assay in the 90 dogs sensitized with housedust mites, antigenic proteins of housedust mites recognized by IgE antibodies were with the apparent molecular masses of 15, 76, 90, 98, and 170-kD. Among them, the 15-kD protein that might be ident ical to Group 2 antigens (Der f2, Der p2) was prominently observed (52/90). This study indicates that about a half of dogs with AD were sensitized to housedust mites, suggesting that Group 2 antigens of housedust mites may be a major allergen in canine AD. KEY WORDS: allergen, atopic dermatitis, canine, housedust mite, IgE.

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“…The rDer f 11 was expressed as a GST fusion protein in Escherichia coli and purified as previously described [16]. The monoclonal antibody Df642 [13]was kindly provided by Dr. L.C. Tsai (Veterans General Hospital, Taipei, Taiwan).…”

Section: Methodsmentioning

confidence: 99%

“…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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Isolation and characterization of a novel 98-kd Dermatophagoides farinae mite allergen

Cited by 61 publications

References 35 publications

Immunization of Rabbits with NematodeAscaris lumbricoidesAntigens Induces Antibodies Cross-Reactive to House Dust MiteDermatophagoides farinaeAntigens

Immunization of Rabbits with NematodeAscaris lumbricoidesAntigens Induces Antibodies Cross-Reactive to House Dust MiteDermatophagoides farinaeAntigens

Determination of Antigenic Proteins of Housedust Mites in 90 Dogs Suffering from Atopic Dermatitis.

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

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