The cat lipocalin Fel d 7 and its cross‐reactivity with the dog lipocalin Can f 1

Apostolović, Danijela; Sánchez-Vidaurre, Sara; Wadén, Konrad; Curin, Mirela; Grundström, Jeanette; Gafvelin, Guro; Veličković, Tanja Ćirković; Grönlund, Hans; Thomas, Wayne R.; Valenta, Rudolf; Hamsten, Carl; Hage, Marianne van

doi:10.1111/all.12955

Cited by 47 publications

(50 citation statements)

References 19 publications

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“…We are also aware that the results from our real-life economic study are applicable only for pollen AIT in Kazakhstan and cannot be generalized, but it has been shown for southern parts of Europe that allergen molecule-based testing would have changed AIT prescription also in these regions substantially [10,11]. So far no studies are available which have analyzed how allergen molecule-based diagnosis would affect AIT prescriptions for indoor allergen sources, but several studies have shown that molecular diagnosis is also more precise in identifying sensitizing indoor allergen sources as compared to allergen extract-based diagnosis [31,32,33]. Should further studies in different populations, regions, and different allergen sources show a similar cost-efficacy of molecular allergen-based diagnosis over allergen extract-based diagnosis for AIT prescription, molecular allergy diagnosis will become standard practice and help to reduce the continuously exploding health care costs for allergic diseases.…”

Section: Discussionmentioning

confidence: 99%

Greater Real-Life Diagnostic Efficacy of Allergen Molecule-Based Diagnosis for Prescription of Immunotherapy in an Area with Multiple Pollen Exposure

Saltabayeva¹,

Garib²,

Morenko³

et al. 2017

Int Arch Allergy Immunol

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Background: Allergen molecule-based diagnosis has been suggested to facilitate the identification of disease-causing allergen sources and the prescription of allergen-specific immunotherapy (AIT). The aim of the current study was to compare allergen molecule-based IgE serology with allergen extract-based skin testing for the identification of the disease-causing allergen sources. The study was conducted in an area where patients are exposed to pollen from multiple sources (trees, grasses, and weeds) at the same time to compare the diagnostic efficiency of the 2 forms of diagnosis. Methods: Patients from Astana, Kazakhstan, who suffered from pollen-induced allergy (n = 95) were subjected to skin prick testing (SPT) with a local panel of tree pollen, grass pollen, and weed pollen allergen extracts and IgE antibodies specific for marker allergen molecules (nArt v 1, nArt v 3, rAmb a 1, rPhl p 1, rPhl p 5, rBet v 1) were measured by ImmunoCAP. Direct and indirect costs for diagnosis based on SPT and marker allergen-based IgE serology as well as direct costs for immunotherapy depending on SPT and serological test results were calculated. Results: The costs for SPT-based diagnosis per patient were lower than the costs for allergen molecule-based IgE serology. However, allergen molecule-based serology was more precise in detecting the disease-causing allergen sources. A lower number of immunotherapy treatments (n = 119) was needed according to molecular diagnosis as compared to extract-based diagnosis (n = 275), which considerably reduced the total costs for diagnosis and for a 3-year treatment from EUR 1,112.30 to 521.77 per patient. Conclusions: The results from this real-life study show that SPT is less expensive than allergen molecule-based diagnostic testing, but molecular diagnosis allowed more precise prescription of immunotherapy which substantially reduced treatment costs and combined costs for diagnosis and treatment.

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Section: Discussionmentioning

confidence: 99%

Greater Real-Life Diagnostic Efficacy of Allergen Molecule-Based Diagnosis for Prescription of Immunotherapy in an Area with Multiple Pollen Exposure

Saltabayeva¹,

Garib²,

Morenko³

et al. 2017

Int Arch Allergy Immunol

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“…Allergen-specific basophil degranulation was analyzed by monitoring the basophil activation markers CD203c and CD63 as previously described 41 . Heparinized venous blood samples from four red meat-allergic patients (IgE range 5.2–>100 kU A /l against α-Gal, see Table S1) and one non-allergic individual were analyzed with BTG, α-Gal peptides obtained after 1 h of gastric phase and pepsin from porcine mucosa as control.…”

Section: Methodsmentioning

confidence: 99%

Peptidomics of an in vitro digested α-Gal carrying protein revealed IgE-reactive peptides

Apostolović

Krstic

Mihailović

et al. 2017

Sci Rep

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The mammalian carbohydrate galactose-α1,3-galactose (α-Gal) causes a novel form of food allergy, red meat allergy, where patients experience severe allergic reactions several hours after red meat consumption. Here we explored gastric digestion of α-Gal glycoproteins using an in vitro model. Bovine thyroglobulin (BTG), a typical α-Gal carrying glycoprotein, was digested with pepsin. The resulting peptides were characterised by SDS PAGE, immunoblot and ImmunoCAP using sera from 20 red meat allergic patients. During pepsinolysis of BTG, a wide range of peptide bands was observed of which 14 to 17 kDa peptides remained stable throughout the gastric phase. The presence of the α-Gal epitope on the obtained peptides was demonstrated by an anti-α-Gal antibody and IgE from red meat allergic patients. The α-Gal digests were able to inhibit up to 86% of IgE reactivity to BTG. Importantly, basophil activation test demonstrated that the allergenic activity of BTG was retained after digestion in all four tested patients. Mass spectrometry-based peptidomics revealed that these peptides represent mostly internal and C-terminal parts of the protein, where the most potent IgE-binding α-Gal residues were identified at Asn1756, Asn1850 and Asn2231. Thus allergenic α-Gal epitopes are stable to pepsinolysis, reinforcing their role as clinically relevant food allergens.

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“…Several studies tested cross reactivity in this group of allergens [8] [11] [12]. Can f 1 and Fel d 7 allergens share a 60% of identity in their amino acid sequences and cross reactivity have been demonstrated experimentally [13]. Although both allergens were part of the group B, we found only a 28% of identity between these lipocalins, a low grade of identity to expect cross-reactivity.…”

Section: Discussionmentioning

confidence: 58%

In <i>Silico</i> Analysis of Cross Reactivity between Lipocalin of Domestic Animals*

Múnera¹,

Andres²,

Sánchez³

et al. 2018

OJI

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Lipocalins are one of the groups of allergens derived from domestic animals with clinical importance for the development of allergic responses. They have been characterized in different animals. With allergenic capacity characterized, little is known about the epitopes involved in allergic responses. Here, potential antigenic regions involved in cross-reactivity among lipocalins were explored through bioinformatics tools. The amino acid sequences of several lipocalins from different domestic animals (mouse, dog, cat, bull, hamster, horse and pig) were used to determine the degree of kinship by phylogenetic studies. Groups with highest phylogenetic relation were obtained by using MEGA software. 3D models of lipocalins not reported in the protein data bank were modeled by homology to identify potential antigenic regions compromised in the cross-reactivity of this group of allergens. The alignment of the entire database of allergenic lipocalins and the inferred maximum likelihood tree segregate lipocalins into five monophyletic clades (referenced here as A, B, C, D and E). According to the multiple pairing analyzes, group C (Fel d 4, Rat n 1 and Equ c 1) showed the highest degree of identity among their amino acid sequences (58%). The analysis of conserved and exposed residues showed that group C shares three antigenic regions that could potentially contribute to its cross-reactivity. Potential antigenic sites were identified for the generation of cross-reactivity between the different lipocalins analyzed in this study. These studies support the need to carry out directed mutagenesis tests to confirm their relevance in the allergenic capacity of lipocalins.

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The cat lipocalin Fel d 7 and its cross‐reactivity with the dog lipocalin Can f 1

Cited by 47 publications

References 19 publications

Greater Real-Life Diagnostic Efficacy of Allergen Molecule-Based Diagnosis for Prescription of Immunotherapy in an Area with Multiple Pollen Exposure

Greater Real-Life Diagnostic Efficacy of Allergen Molecule-Based Diagnosis for Prescription of Immunotherapy in an Area with Multiple Pollen Exposure

Peptidomics of an in vitro digested α-Gal carrying protein revealed IgE-reactive peptides

In <i>Silico</i> Analysis of Cross Reactivity between Lipocalin of Domestic Animals*

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The cat lipocalin Fel d 7 and its cross‐reactivity with the dog lipocalin Can f 1

Cited by 47 publications

References 19 publications

Greater Real-Life Diagnostic Efficacy of Allergen Molecule-Based Diagnosis for Prescription of Immunotherapy in an Area with Multiple Pollen Exposure

Greater Real-Life Diagnostic Efficacy of Allergen Molecule-Based Diagnosis for Prescription of Immunotherapy in an Area with Multiple Pollen Exposure

Peptidomics of an in vitro digested α-Gal carrying protein revealed IgE-reactive peptides

In &lt;i&gt;Silico&lt;/i&gt; Analysis of Cross Reactivity between Lipocalin of Domestic Animals*

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In <i>Silico</i> Analysis of Cross Reactivity between Lipocalin of Domestic Animals*