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Purpose: Divergent results on the IgE reactivity of dog-allergic subjects to Can f 4 have been reported. The aim of this study was to evaluate the significance of Can f 4 in dog allergy and to develop an immunochemical method for measuring Can f 4 content in environmental samples.
Methods: We purified the natural dog allergen Can f 4 from a dog dander extract by monoclonal antibody-based affinity chromatography and generated its variant in a recombinant form. Sixty-three dog-allergic patients and 12 nonallergic control subjects were recruited in the study. The IgE-binding capacity of natural Can f 4 and its recombinant variant was assessed by ELISA, immunoblotting, and skin prick tests (SPT).
Results: Eighty-one percent of the dog-allergic patients showed a positive result to the immunoaffinity-purified natural Can f 4 in IgE ELISA, but only 46% in IgE immunoblotting. Respective results with the recombinant Can f 4 variant were 54% and 49%. SPT results reflected those obtained in ELISA and immunoblotting. The overall IgE reactivity of the immunoaffinity-purified natural Can f 4 was found to depend strongly on the integrity of the allergen's conformation. A sandwich ELISA based on monoclonal antibodies was found to be functional for measuring Can f 4 in environmental samples.
Conclusions: Can f 4 is a major allergen of dog together with Can f 1 and Can f 5. In combination with other dog allergens, it improves the reliability of allergy tests in dog allergy.
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http://dx.doi.org/10.4168/aair.2015.7.4.384 | DOI Listing |
J Asthma Allergy
December 2024
Department of Allergy, Beijing Key Laboratory of Precision Medicine for Diagnosis and Treatment on Allergic Diseases, National Clinical Research Center for Dermatologic and Immunologic Diseases, Peking Union Medical College Hospital, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, 100730, People's Republic of China.
Pollen-food allergy syndrome is an IgE-mediated allergic reaction arising from cross-reactive homologous allergens found in both food and pollen. Allergens, such as pathogenesis-related protein class 10 and profilin, usually trigger oropharyngeal itching and numbness in patients, whereas lipid transfer proteins tend to induce anaphylaxis. This article presents a case study of an individual with Artemisia pollen allergy who experienced anaphylaxis after consuming red fruit ginseng, a perennial herb belonging to the Campanulaceae family.
View Article and Find Full Text PDFWorld Allergy Organ J
December 2024
Institute of Allergy, Yonsei University College of Medicine, Seoul, South Korea.
Background: The diagnosis of the culprit allergen depends on exposure, symptoms at exposure, and the presence of specific IgE (sIgE). Pet allergens are sticky and can sensitize individuals without adoption history. Exclusive dog owners frequently exhibit both dog (e5) and cat dander sIgE (e1).
View Article and Find Full Text PDFFood Chem
December 2024
REQUIMTE-LAQV, Faculdade de Farmácia, Universidade do Porto, Rua de Jorge Viterbo Ferreira, 228, 4050-313 Porto, Portugal. Electronic address:
Edible insects are attracting increasing interest as sustainable alternative protein sources. Despite being considered a safe food for most population, their consumption can pose health risks for allergic patients. This work focused on isolating proteins from the four-European Union approved insects (Tenebrio molitor, Alphitobius diaperinus, Acheta domesticus, and Locusta migratoria) and evaluating their potential immunoglobulin E (IgE)-reactivity with crustacean-allergic patients' sera.
View Article and Find Full Text PDFJ Agric Food Chem
December 2024
College of Ocean Food and Biological Engineering, Jimei University, Xiamen, Fujian 361021, China.
Arginine kinase (AK) from the phosphagen kinase family is a cross-reactive shellfish allergen. Structurally related cross-reactive allergens are involved in the pathogenesis of allergic symptoms. This study aimed to unravel the cross-reactivity of AK from a structural perspective.
View Article and Find Full Text PDFRegulatory T cells (Tregs) actively engage in immune suppression to prevent autoimmune diseases but also inhibit anti-tumor immunity. Although Tregs express a TCR repertoire with relatively high affinities to self, they are normally quite stable and their inflammatory programs are intrinsically suppressed. We report here that diacylglycerol (DAG) kinases (DGK) ( and ( are crucial for homeostasis, suppression of proinflammatory programs, and stability of Tregs and for enforcing their dependence on CD28 costimulatory signal.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!