Background: Seafood allergy has been related to mite sensitization, mainly mediated by the muscle protein tropomyosin.
Objectives: To determine the correlation between seafood hypersensitivity and mite sensitization (Dermatophagoides pteronyssinus and Chortoglyphus arcuatus, a highly prevalent storage mite in Spain) and to investigate the implication of tropomyosin in cross-reactivity.
Methods: Patients from Northwest Spain were divided into 2 groups. The mite-seafood group contained 30 allergic mite individuals with a clinical history of food hypersensitivity. The mite group contained 40 individuals with positive skin prick test results to D pteronyssinus and C arcuatus but negative seafood test results. Specific IgE (sIgE) to whole mite and shrimp extracts, mite tropomyosin (rDer p 10), and shrimp tropomyosin (rPen a 1) were determined in each serum sample. Allergenic profiles were analyzed by immunoblot. Cross-reactivity studies were investigated by enzyme-linked immunosorbent assay and immunoblot inhibition studies.
Results: In the mite-seafood group, 71% of patients had positive sIgE results to shrimp and 55% of them to shrimp tropomyosin. A strong correlation was found between sIgE to shrimp tropomyosin and mite tropomyosin. Positive correlation was observed between sIgE to shrimp tropomyosin and severity of symptoms. In the mite group, none of the 20% of patients with sIgE to shrimp tested positive to shrimp tropomyosin. In the immunoblot inhibition experiment, the shrimp extract was totally inhibited by mite extract. These data suggest that primary sensitization is related to mite sensitization.
Conclusion: Tropomyosin does not seem to be the main allergen involved in mite-seafood sensitization in mite sensitized individuals. High levels of sIgE to tropomyosin seem to be related to severity of symptoms.
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http://dx.doi.org/10.1016/j.anai.2010.11.014 | DOI Listing |
Food Chem
December 2024
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; Academy of Contemporary Food Engineering, South China University of Technology, Guangzhou Higher Education Mega Centre, Guangzhou 510006, China; Engineering and Technological Research Centre of Guangdong Province on Intelligent Sensing and Process Control of Cold Chain Foods, & Guangdong Province Engineering Laboratory for Intelligent Cold Chain Logistics Equipment for Agricultural Products, Guangzhou Higher Education Mega Centre, Guangzhou 510006, China; Food Refrigeration and Computerized Food Technology (FRCFT), Agriculture and Food Science Centre, University College Dublin, National University of Ireland, Belfield Dublin 4, Ireland. Electronic address:
Graphene oxide (GO), renowned for its two-dimensional structure and exceptional fluorescence quenching capabilities, is a preferred choice for the construction of fluorescence biosensors. As the sensitivity demands for these sensors escalate, enhancing the fluorescence quenching performance of GO and reducing background fluorescence become paramount to optimize the sensor sensitivity. In this study, the use of cold plasma (CP) treatment with glucose solution as a reducing agent to refine GO into reduced graphene oxide (r-GO) with optimal fluorescence quenching abilities was explored.
View Article and Find Full Text PDFEJHaem
December 2024
Department of Internal Medicine, Division of Clinical Immunology and Allergy, Department of Nephrology and Transplantation, Amsterdam Institute for Immunology and Infectious Diseases Amsterdam University Medical Center, University of Amsterdam Amsterdam the Netherlands.
Background: Transfusion reactions occur at an estimated incidence of 2 per 1.000 transfused products. Anaphylactic transfusion reactions are rarer, and seen in 1 per 10.
View Article and Find Full Text PDFJ Agric Food Chem
December 2024
Department of Health, Nutrition, and Food Sciences, Florida State University, Tallahassee, Florida 32306, United States.
Bony fish is one of the big-nine allergenic foods in the US. This study established a monoclonal antibody (mAb)-based indirect competitive enzyme-linked immunosorbent assay (ELISA) for the detection of bony fish tropomyosin (TM), a fish allergen. Immunoassay (Western blot and ELISA) was performed to characterize anti-TM mAb8F5 (target configuration, immunoaffinity, and species selectivity).
View Article and Find Full Text PDFFish Shellfish Immunol
January 2025
College of Marine and Environmental Sciences, Tianjin University of Science and Technology, Tianjin, 300457, China. Electronic address:
Food Funct
December 2024
College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Jimei University, Xiamen, Fujian 361021, China.
Tropomyosin (TM) has been determined as the major allergen in . However, little information is available about its antigenic epitopes and cross-reactivity. In this study, recombinant TM was obtained through genetic engineering and its IgG-/IgE-binding activity was similar to native TM.
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