Identification, characterization, and cloning of a complementary DNA encoding a 60-kd house dust mite allergen (Der f 18) for human beings and dogs

Weber, Eric; Hunter, S W; Stedman, Kim E.; Dreitz, Steve; Olivry, Thierry; Hillier, Andrew; McCall, Catherine

doi:10.1067/mai.2003.1602

Cited by 65 publications

(68 citation statements)

References 20 publications

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“…This allergen is a glycosylated protein comprising 437 amino acids, with a native molecular weight of 50 kDa. Puriϐied Der f 18 identiϐied 57 to 77% of sera from dogs sensitized to DEF (Weber et al 2003). Like Der f 15, this protein showed homology to insect chitinases and was detected in the mite digestive system, but not in fecal pellets.…”

Section: Discussionmentioning

confidence: 94%

“…However, only few allergens have been identiϐied in dogs. The most important are: Der p 1 (25 kDa) and Der p 2 (14 kDa) from DEP, and Der f 1 (25 kDa), Der f 2 (14 kDa), Der f 10 (37 kDa), Der f 15 (98 kDa) and Der f 18 (60 kDa) from DEF (Noli et al 1996, McCall et al 2001, Weber et al 2003.…”

Section: Discussionmentioning

confidence: 99%

“…One DEF protein of 60 kDa, called Der f 18, has been identiϐied in a previous study as a major allergen for dogs (Weber et al 2003). This allergen is a glycosylated protein comprising 437 amino acids, with a native molecular weight of 50 kDa.…”

Section: Discussionmentioning

confidence: 99%

“…Using immunoassays, some DEF and DEP allergens have been identiϐied in sera of dogs with CAD (Noli et al 1996, McCall et al 2001, Weber et al 2003 (Table 2). No such studies have so far been conducted in Brazil and since the pattern of antigen recognition may vary between dog populations due to genetic and environmental differences, the identiϐication of the antigen recognition pattern in Brazilian dogs is of major importance.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

2012

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“…Similarly, expansin-like proteins of major grass allergen groups II and III bear homology to the CBM portion of b-expansin (9,10). Other potent allergens (mite, olive, latex, and fruits) also contain a CBM, suggesting it has a critical role in prompting allergic responses (10)(11)(12)(13)(14).…”

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confidence: 99%

Oxidized Cellulose Binding to Allergens with a Carbohydrate-Binding Module Attenuates Allergic Reactions

Shani

Shani²,

Shoseyov

et al. 2011

The Journal of Immunology

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Grass and mite allergens are of the main causes of allergy and asthma. A carbohydrate-binding module (CBM) represents a common motif to groups I (β-expansin) and II/III (expansin-like) grass allergens and is suggested to mediate allergen-IgE binding. House dust mite group II allergen (Der p 2 and Der f 2) structures bear strong similarity to expansin's CBM, suggesting their ability to bind carbohydrates. Thus, this study proposes the design of a carbohydrate-based treatment in which allergen binding to carbohydrate particles will promote allergen airway clearance and prevent allergic reactions. The aim of the study was to identify a polysaccharide with high allergen-binding capacities and to explore its ability to prevent allergy. Oxidized cellulose (OC) demonstrated allergen-binding capacities toward grass and mite allergens that surpassed those of any other polysaccharide examined in this study. Furthermore, inhalant preparations of OC microparticles attenuated allergic lung inflammation in rye grass-sensitized Brown Norway rats and OVA-sensitized BALB/c mice. Fluorescently labeled OC efficiently cleared from the mouse airways and body organs. Moreover, long-term administration of OC inhalant to Wistar rats did not result in toxicity. In conclusion, many allergens, such as grass and dust mite, contain a common CBM motif. OC demonstrates a strong and relatively specific allergen-binding capacity to CBM-containing allergens. OC's ability to attenuate allergic inflammation, together with its documented safety record, forms a firm basis for its application as an alternative treatment for prevention and relief of allergy and asthma.

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Allergens and Environmental Influence

Prélaud¹

2013

Veterinary Allergy

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Identification, characterization, and cloning of a complementary DNA encoding a 60-kd house dust mite allergen (Der f 18) for human beings and dogs

Cited by 65 publications

References 20 publications

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

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

Oxidized Cellulose Binding to Allergens with a Carbohydrate-Binding Module Attenuates Allergic Reactions

Allergens and Environmental Influence

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