Studies on allergens of mammalian origin

Calam, D.H.; Davidson, J.; Ford, Anna

doi:10.1016/s0021-9673(01)93688-x

Cited by 12 publications

(10 citation statements)

References 10 publications

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“…These allergens are present in dog serum as well as in epithelial extracts [22, 36, 37, 38, 42, 45, 51, 52, 53]. The sequence of dog albumin has been determined and the recombinant protein was expressed as IgE–reactive protein in E. coli [54].…”

Section: Allergen Sources Allergensmentioning

confidence: 99%

“…Therefore, studies were carried out to investigate the presence of cross–reactive antigens/allergens in dog and cat extracts in order to explain the clinical observation that dog allergy is frequently associated with cat allergy [14, 22, 40, 53]. Brandt et al [124]described the presence of IgE antibodies to cat allergens present in 70% of dog allergic patients.…”

Section: Ige–cross–reactivities With Animal Allergens: the Nature Of mentioning

confidence: 99%

“…Albumins represent the most conserved family of cross–reactive mammalian allergens [22, 40, 47, 53]. Other serum proteins (e.g.…”

Section: Ige–cross–reactivities With Animal Allergens: the Nature Of mentioning

confidence: 99%

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Allergy to Mammalian Proteins: At the Borderline between Foreign and Self?

Spitzauer

1999

Int Arch Allergy Immunol

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Atopic individuals are characterized by their genetically determined tendency to mount IgE antibody responses against otherwise harmless antigens. Many of the environmental allergens (e. g., plant–, insect–, mould–derived allergens) are recognized as foreign intruders by the immune system. However, a substantial proportion of atopic individuals mount IgE responses to allergens of mammalian origin and, as recently reported, certain of them even react with human proteins (i. e., autoallergens). Through the application of molecular biological techniques for allergen characterization, the molecular nature and biological function of an increasing number of mammalian allergens have been revealed. This review provides a summary of well characterized mammalian allergens derived from hair/dander, saliva, serum and urine of animals (cat, dog, rodents, cow, horse) as well as of some recently characterized autoallergens. In addition, mammalian allergens were grouped in protein families with similar sequences and/or biological functions. The importance of cross–reactivities is exemplified for albumins which represent abundant mammalian serum proteins and highly cross–reactive allergens. Finally, possible advantages of using recombinant animal allergens for novel forms of component–resolved diagnosis and treatment of allergies to mammalian proteins are described.

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Section: Allergen Sources Allergensmentioning

confidence: 99%

Section: Ige–cross–reactivities With Animal Allergens: the Nature Of mentioning

confidence: 99%

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Allergy to Mammalian Proteins: At the Borderline between Foreign and Self?

Spitzauer

1999

Int Arch Allergy Immunol

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“…As with all allergens extracts examined, dog hair/ dander extract comprises a complex mixture of proteins of different molecular weights [10]. Theoretically all of these, if encountered in appropriate quantities, have lhe potential of acting as allergens.…”

Section: Introduetionmentioning

confidence: 99%

The allergens of dog. I. Identification using crossed radio‐immunoelectrophoresis

Ford

Alterman

Kemeny

1989

Clin Experimental Allergy

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The antigens present in an extract of dog hair and dander were examined by crossed immunoelectrophoresis (CIE) and the IgE-binding allergens by crossed radio-immunoelectrophoresis (CRIE), respectively, using sera from 60 British and Finnish animal-allergic subjects. The extract was comprised of a minimum of 28 antigens, 11 of which were common to dog serum. IgE antibody in the sera of the dog-sensitive patients bound to 21 of the 28 antigens at varying frequencies and intensities. Binding of any intensity occurred most frequently to two serum proteins: antigen 23 (IgG) binding IgE in 88% of cases, and antigen 3 (dog serum albumin, DSA) in 77% of cases. Dander antigen 8 bound in 63% and antigen 1 in 42% of the sera. Strong IgE binding, however, was most commonly associated with dander antigen 8 followed by antigens 1 and 23 (IgG) then 3 (DSA). The ranking of the antigens as allergens was similar for the two populations except that DSA was more important for the British than for the Finnish subjects.

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“…When gel filtration on HPLC is followed by ident ification of allergens using immunological methods, this becomes an analytical 2-dimensional technique with a high degree of resolution. The combination of gel filtration on a HPLC column and radioallergo sorbent test (RAST) has earlier been investigated by Calam et al [1984] as a method for screening extracts for immunologically reactive components. Compared to traditional crossed radioimmunoelectrophoresis (CRIE) [ Weeke and Lowenstein, 1973], which is often used to characterize allergen preparations, this system gives the additional information on molecular size distribution.…”

Section: Introductionmentioning

confidence: 99%

High-Performance Liquid Chromatography of <i>Cladosporium herbarum</i>

Landmark¹,

Aukrust²

1985

Int Arch Allergy Immunol

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High-performance liquid chromatography (HPLC) using a gel permeation column was applied to separate components in a crude extract of the mould Cladosporium herbarum. Allergenic activity as well as individual allergens in collected fractions were analyzed by direct radioallergosorbent test (RAST) and fused rocked radioimmunoelectrophoresis (FRRIE), respectively. Thus, information of the molecular weight as well as the importance of the individual allergens were obtained simultaneously in a system showing a high degree of resolution. The study demonstrated that the crude extract of C.herbarum contained allergens mainly in the molecular weight range between 10,000 and 300,000 daltons. The results demonstrated the importance of carrying out both RAST and FRRIE to detect all allergens.

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Studies on allergens of mammalian origin

Cited by 12 publications

References 10 publications

Allergy to Mammalian Proteins: At the Borderline between Foreign and Self?

Allergy to Mammalian Proteins: At the Borderline between Foreign and Self?

The allergens of dog. I. Identification using crossed radio‐immunoelectrophoresis

High-Performance Liquid Chromatography of <i>Cladosporium herbarum</i>

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