Molecular Characterization of the Group 4 House Dust Mite Allergen from Dermatophagoides pteronyssinus and Its Amylase Homologue from Euroglyphus maynei

Mills, K.L.; Hart, Barbara; Lynch, Neil R.; Thomas, Wayne R.; Smith, Wendy-Anne

doi:10.1159/000024227

Cited by 33 publications

(28 citation statements)

References 21 publications

(43 reference statements)

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“…The 19-residue N-terminal sequence however only had weak homology to other amylases because this is a region of sequence variation. cDNA cloning of Der p 4 and Eur m 4 revealed that the allergens were 496-amino-acid residue α-amylases with a calculated MW of 57,000 [151]. The sequence contained all of the conserved regions known to be important for amylase structure, calcium binding, substrate and catalytic activity.…”

Section: Group 4 Allergensmentioning

confidence: 99%

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: Group 4 Allergensmentioning

confidence: 99%

Characterization and Immunobiology of House Dust Mite Allergens

Thomas¹,

Smith²,

Hales³

et al. 2002

Int Arch Allergy Immunol

303

254

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“…One allergen of 56 kDa, called Blo t 4, has been described as a minor allergen for humans and possesses α-amylase activity. α-Amylases are potent and highly conserved allergens found in mites, fungi, and cereals (Mills et al 1999). …”

Section: Discussionmentioning

confidence: 99%

Serological identification of house dust mite allergens in dogs with atopic dermatitis

2012

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Pesq. Vet. Bras. 32(9):917-921, setembro 2012 917 RESUMO.-[Identiϐicação sorológica de alérgenos de ácaros da poeira domiciliar em cães com dermatite atópica.] Antígenos de ácaros da poeira domiciliar são utilizados por décadas para diagnóstico de doenças alér-gicas em seres humanos e animais. O objetivo do presente trabalho foi identiϐicar proteínas alergênicas presentes em extratos de Dermatophagoides farinae e Blomia tropicalis através de "immunoblotting" utilizando-se soros de animais alérgicos e conjugado anti-IgE canina. A análise por "immunoblotting" dos antígenos presentes no extrato de D. farinae (FDA Allergenic), utilizando soros de dez animais alérgicos, mostrou que oito soros reconhecem uma banda com peso molecular de aproximadamente 102 kDa; oito soros duas bandas entre 52 e 76 kDa; cinco soros uma banda com aproximadamente 76 kDa; quatro soros uma ban- House dust mite antigens have been used for decades to diagnose allergic diseases in humans and animals. The objective of this study was to identify allergens in commercial Dermatophagoides farinae and Blomia tropicalis extracts by immunoblotting using sera from allergic dogs and anti-dog IgE conjugate. The analysis of antigens present in the D. farinae extract (FDA Allergenic) using sera from 10 dogs allergic to D. farinae showed that eight sera recognized a band of approximately 102 kDa, eight recognized two bands of 52 to 76 kDa, ϐive recognized one band of approximately 76 kDa, four recognized one band of 31 to 38 kDa, and two recognized one band of 12 to 17 kDa. Immunoblot assays of the B. tropicalis extract (FDA Allergenic) using sera from 10 animals allergic to B. tropicalis showed that ϐive sera recognized two bands of 52 to 76 kDa. These results demonstrate the importance of the two house dust mite species for the pathogenesis of canine atopic dermatitis in Brazil. In addition, the results indicate which allergens should be present in allergenic extracts used for diagnosis and allergen-speciϐic immunotherapy. da entre 31 e 38 kDa; e dois soros uma banda entre 12 e 17 kDa. A análise por "immunoblotting" dos antígenos do extrato de B. tropicalis (FDA Allergenic) mostrou que cinco soros reconhecem duas bandas com pesos moleculares entre 52 e 76 kDa. Esses resultados demonstram a importância dessas duas espécies de ácaros da poeira domiciliar na patogênese da dermatite atópica canina no Brasil, assim como indicam alérgenos que devem estar presentes nos extratos alergênicos utilizados para diagnóstico e imunoterapia alérgeno-especíϐica.

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“…The house dust mite α-amylase showed positive IgE reactivity with 46% of mite-allergic adults and 25% of mite-allergic children. In 1999, Mills et al [7] cloned the genes encoding for the α-amylase from D. pteronyssinus and E. maynei, respectively. The mature Der p 4 and Eur m 4 proteins share about 90% amino acid sequence homology.…”

Section: Discussionmentioning

confidence: 99%

“…α-Amylases contain several well-defined regions in their amino acid sequences that are highly conserved across a broad spectrum of organisms that are of evolutionary distinct origins. Group 4 allergens from Dermatophagoides pteronyssinus and Euroglyphus maynei have been shown to contain some of these conserved regions [7]. The 10 recognized invariant residues within these conserved regions include 7 thought to be involved in catalysis and substrate binding in the active site and 3 that are structurally important, and they are present in both species.…”

Section: Introductionmentioning

confidence: 99%

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Mite Amylase from <i>Blomia tropicalis</i> (Blo t 4): Differential Allergenicity Linked to Geographical Regions

Cheong

Ramos

Tang

et al. 2008

Int Arch Allergy Immunol

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Background:Blomia tropicalis is an important domestic dust mite in the tropics and subtropics. This study describes cDNA cloning of the group 4 allergen of B. tropicalis, and the evaluation of the sensitization of this allergen in atopic populations from 2 geographic regions. Methods: cDNA cloning was carried out using the Smart RACE cDNA amplification kit. The full-length Blo t 4 cDNA was isolated by cDNA library screening, 5′ and 3′ rapid amplification of cDNA ends and long-distance PCR. Sequence analysis was performed with a combination of the Clustal W, CGC and Blast program packages. The cDNA was expressed in Pichia pastoris yeast. The skin prick test was used to evaluate the sensitization profile of recombinant Blo t 4, crude dust mite allergen extracts and major B. tropicalis recombinant allergen Blo t 5. Results: The cloned Blo t 4 had a molecular weight of 56 kDa and had 68% amino acid homology with group 4 allergens of Dermatophagoides pteronyssinus and 65% with those of Euroglyphus maynei. A sensitization profile to the expressed recombinant Blo t 4 allergen (28%) showed an unusually higher frequency than to the major allergen Blo t 5 (22%) in allergic subjects from Chengdu, PR China. In comparison, the subjects from Singapore showed very low sensitization to Blo t 4 (4%) compared with Blo t 5 (84%). Conclusions: Group 4 allergens of B. tropicalis may be an important dust mite allergen in certain distinct populations.

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Molecular Characterization of the Group 4 House Dust Mite Allergen from Dermatophagoides pteronyssinus and Its Amylase Homologue from Euroglyphus maynei

Cited by 33 publications

References 21 publications

Characterization and Immunobiology of House Dust Mite Allergens

Characterization and Immunobiology of House Dust Mite Allergens

Serological identification of house dust mite allergens in dogs with atopic dermatitis

Mite Amylase from <i>Blomia tropicalis</i> (Blo t 4): Differential Allergenicity Linked to Geographical Regions

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