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Construction of a Hybrid Vaccine Based on Der f 35-Derived Peptides with Reduced Allergenicity.
Int Arch Allergy Immunol
November 2024
Department of Clinical Laboratory, The Second Affiliated Hospital of Nantong University, Nantong, China.
Introduction: House dust mite is the primary trigger of allergic respiratory diseases worldwide, and allergen-specific immunotherapy (AIT) is the only disease-modifying treatment in the clinic. The use of allergen molecules instead of extracts is a promising strategy in AIT. In this study, we constructed a peptide hybrid vaccine against the major mite allergen Der f 35 and verified its hypoallergenicity, making it to be a promising candidate for AIT of mite allergy.
View Article and Find Full Text PDFDevelopment of Cashew and Pistachio Ladders through a Food-Processing Approach.
Foods
October 2024
School of Chemical Engineering, University of New South Wales, Kensington, NSW 2052, Australia.
Following successful oral immunotherapy (OIT) for peanut allergy using boiled peanuts (BOPI trial), this study investigated the potential of wet-thermal-processing-induced allergen modification, specifically soaking and boiling (1-4 h) to reduce the allergenicity of cashew and pistachio allergens. In addition, this study provides a foundation of understanding for developing safer forms of cashew/pistachio administration for application in OIT by gradual exposure to increasing doses of modified allergens with reduced potency as an "allergen ladder". An SDS-PAGE analysis and an intrinsic-fluorescence spectroscopy revealed altered tertiary structures of the allergens, leading to their denaturation and even degradation.
View Article and Find Full Text PDFTherapeutic potential of a novel hybrid protein: Mitigating allergy and airway remodeling in chronic asthma models induced by Dermatophagoides pteronyssinus.
Mol Immunol
November 2024
Laboratory of Allergology and Acarology (LAA), Institute of Health Sciences, Federal University of Bahia, Salvador, BA, Brazil; Post-Graduate Program in Immunology (PPGIm) of the Federal University of Bahia, Salvador, BA, Brazil. Electronic address:
Background: The house-dust mite Dermatophagoides pteronyssinus is a key trigger of allergic asthma. Therefore, it is essential to develop new vaccines that can alter inflammatory processes and airway remodeling. The goal of this study was to test the hypoallergenic and immunogenic characteristics of the hypoallergen rDer p 2231 in a murine model of chronic asthma induced by D.
View Article and Find Full Text PDFB cell memory of Immunoglobulin E (IgE) antibody responses in allergy.
Curr Opin Immunol
December 2024
Jaffe Food Allergy Institute, Division of Allergy and Immunology, Department of Pediatrics, and Lipschultz Precision Immunology Institute, Department of Immunology and Immunotherapy, Icahn School of Medicine at Mount Sinai, New York, NY, USA. Electronic address:
Immunoglobulin E (IgE)-mediated allergic diseases are driven by high-affinity allergen-specific IgE antibodies. IgE antibodies bind to Fc epsilon receptors on mast cells, prompting their degranulation and initiating inflammatory reactions upon allergen crosslinking. While most IgE-producing plasma cells have short lifespans, and IgE memory B cells are exceedingly rare, studies have indicated that non-IgE-expressing type 2-polarized IgG memory B cells serve as a reservoir of IgE memory in allergies.
View Article and Find Full Text PDFCross-protection of AIT-induced antibodies to related allergens requires a high degree of structural identity.
Allergy
September 2024
Institute of Pathophysiology and Allergy Research, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria.
Background: In contrast to sublingual immunotherapy (SLIT) with recombinant Mal d 1 (rMal d 1-SLIT), SLIT with rBet v 1 (rBet v 1-SLIT) induced Mal d 1-cross-reactive antibodies without IgE-blocking activity. To elucidate whether the development of cross-protective IgG responses depends on the degree of molecular identity of allergens we compared the cross-reactivity, cross-blocking activity, and affinity of SLIT-induced antibodies with allergens of varying amino acid sequence identities to Bet v 1 and Mal d 1, namely Cor a 1.04 (hazelnut), Pru av 1 (cherry), and Dau c 1 (carrot).
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