Molecular and immunological characterization of Can f 4: a dog dander allergen cross‐reactive with a 23 kDa odorant‐binding protein in cow dander

Mattsson, Lars; Lundgren, T. S.; Olsson, Peter; Sundberg, M.; Lidholm, Jonas

doi:10.1111/j.1365-2222.2010.03533.x

Cited by 66 publications

(59 citation statements)

References 21 publications

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“…Q647G9) was produced in Escherichia coli as a hexahistidine-tagged recombinant protein by using a synthetic gene construct and purified by means of immobilized metal ion affinity chromatography followed by ion exchange chromatography, as previously described. 24 Experimental ImmunoCAP Ara h 6 tests were prepared, 25 and IgE levels of 0.35 kU A /L or greater were considered positive.…”

Section: Oral Food Challengementioning

confidence: 99%

Peanut component Ara h 8 sensitization and tolerance to peanut

Asarnoj

Nilsson

Lidholm

et al. 2012

Journal of Allergy and Clinical Immunology

133

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Section: Oral Food Challengementioning

confidence: 99%

Peanut component Ara h 8 sensitization and tolerance to peanut

Asarnoj

Nilsson

Lidholm

et al. 2012

Journal of Allergy and Clinical Immunology

133

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“…No. Q647G9) was produced in Escherichia coli as a hexahistidine-tagged recombinant protein using a synthetic gene construct and purified by immobilized metal ion affinity chromatography followed by ion exchange chromatography as described [20]. Experimental ImmunoCAP tests were prepared as described [21].…”

Section: Introductionmentioning

confidence: 99%

Anaphylaxis to Peanut in a Patient Predominantly Sensitized to Ara h 6

Asarnoj

Glaumann²,

Elfström³

et al. 2012

Int Arch Allergy Immunol

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Diagnosis of peanut allergy has improved thanks to component-resolved diagnostics. Peanut allergen component Ara h 2 is considered to indicate true peanut allergy. The component Ara h 6 is structurally similar to Ara h 2, but the diagnostic value of analyzing IgE antibodies to Ara h 6 is unclear. A boy sensitized (≥0.35 kU_A/l) to Ara h 8 but not to Ara h 1, Ara h 2 and Ara h 3 was challenged with peanut and developed grade II anaphylaxis. In serum collected at the time of challenge a doubling of IgE to the peanut allergen extract was observed compared to allergy testing 9 months earlier. In contrast, IgE levels to Ara h 1, Ara h 2, Ara h 3 and to Ara h 8 were rather unchanged. After another 2 months, Ara h 6 was analyzed and revealed a level of 24 kU_A/l whilst Ara h 2 was 0.12 kU_A/l. We suggest that IgE sensitization to Ara h 6 caused the reaction and conclude that analyses of IgE levels to peanut and peanut components should be performed in connection with a challenge. Furthermore, levels to Ara h 2 below 0.35 kU_A/l may still indicate a risk of severe reaction at the time of challenge since in rare cases, Ara h 6 IgE antibodies may be present without occurrence of IgE antibodies to Ara h 2.

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“…Can f 3, dog serum albumin, is a highly conserved protein, and antibodies directed to Can f 3 cross-react extensively with albumin of other animal species [7]. Approximately 50% of dog-allergic patients present IgE antibodies against Can f 1, 20% against Can f 2 and 15–40% against Can f 3 and Can f 4 [6]. …”

Section: Introductionmentioning

confidence: 99%

“…Among the described dog allergens, Can f 1, Can f 2 and Can f 4 are all members of the lipocalin protein family and have been purified and expressed as recombinant proteins [5,6]. Can f 3, dog serum albumin, is a highly conserved protein, and antibodies directed to Can f 3 cross-react extensively with albumin of other animal species [7].…”

Section: Introductionmentioning

confidence: 99%

Involvement of Can f 5 in a Case of Human Seminal Plasma Allergy

Basagaña

Bartolomé²,

Pastor-Vargas³

et al. 2012

Int Arch Allergy Immunol

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Background: The existence of IgE binding to dog dander extract without IgE antibodies against the described dog allergens (Can f 1, 2, 3 and 4) implies the presence of other dog allergens yet to be identified. Recently, an IgE-binding protein was isolated from dog urine and identified as prostatic kallikrein; it has been named Can f 5. Cross-reactivity between a dog dander allergen and human prostate-specific antigen (PSA) has been described. The aim of this study was to identify the dog dander allergen that presents cross-reactivity with PSA and demonstrate its clinical relevance in our patient with human seminal plasma allergy. Methods: SDS-PAGE immunoblotting and inhibition tests were performed. Mass spectrometry was carried out to identify the protein involved in the allergy reactions. Results: SDS-PAGE immunoblotting-inhibition with an IgE-binding protein from dog prostatic secretion showed total IgE binding inhibition to a 28-kDa IgE-reactive band identified as PSA. The electroeluted protein from dog prostatic secretion was identified by mass spectrometry as Can f 5. IgE immunoblotting of human seminal plasma incubated with the serum of the patient revealed two IgE-binding bands (28 and 32.7 kDa). Both SDS-PAGE immunoblotting inhibition assays, with human seminal plasma or purified PSA in solid phase, showed complete IgE binding inhibition when the serum of the anaphylactic patient was preincubated with dog dander extract or recombinant Can f 5. Conclusions: The dog dander allergen that shows cross-reactivity with human PSA has been characterized and turns out to be the recently described Can f 5. We demonstrated the clinical relevance of this cross-reactivity in a patient.

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Molecular and immunological characterization of Can f 4: a dog dander allergen cross‐reactive with a 23 kDa odorant‐binding protein in cow dander

Abstract: Recombinant Can f 4 brings the panel of available dog allergens closer to completion and will be important in component-resolved diagnostics in allergy to animal epithelial allergens.

Cited by 66 publications

References 21 publications

Peanut component Ara h 8 sensitization and tolerance to peanut

Peanut component Ara h 8 sensitization and tolerance to peanut

Anaphylaxis to Peanut in a Patient Predominantly Sensitized to Ara h 6

Involvement of Can f 5 in a Case of Human Seminal Plasma Allergy

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