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https://www.readbyqxmd.com/read/28231574/biomarkers-in-allergic-airway-disease-simply-complex
#1
Adam M Chaker, Ulrich M Zissler, Martin Wagenmann, Carsten Schmidt-Weber
Clinical diagnoses of allergic airway disease need confirmation of a relevant sensitization to allergens. Serum-based component-resolved diagnosis has become increasingly popular and allows the precise assessment of specific IgE to molecular allergens. Molecular allergen diagnosis has improved our understanding of disease phenotypes in allergic patients, including cross-reactive patterns and food allergy. Beyond sensitization profiles, characterization of the (endo-)type and severity of a local allergic disease is useful for targeted therapy with biologics in advanced allergic airway disease...
February 24, 2017: ORL; Journal for Oto-rhino-laryngology and its related Specialties
https://www.readbyqxmd.com/read/28221944/a-novel-immunoassay-test-system-for-detection-of-modified-allergen-residues-present-in-almond-cashew-coconut-hazelnut-and-soy-based-nondairy-beverages
#2
Jongkit Masiri, Lora Benoit, Mahzad Meshgi, Jeffrey Day, Cesar Nadala, Mansour Samadpour
A growing number of plant-based milk substitutes have become commercially available, providing an array of options for consumers with dietary restrictions. Though several of these products rival cow's milk in terms of their nutritional profiles, beverages prepared with soy and tree nuts can be a significant concern to consumers because of potential contamination with food allergens. Adding to this concern is the fact that allergen residues from plant-based beverages are modified during manufacturing, thereby decreasing the sensitivity of antibody-based detection methods...
September 2016: Journal of Food Protection
https://www.readbyqxmd.com/read/28219072/human-allergen-specific-igg-subclass-antibodies-measured-using-immunocap-technology
#3
Robert Movérare, Karin Blume, Peter Lind, René Crevel, Åsa Marknell DeWitt, Stella Cochrane
BACKGROUND: Knowledge of human IgG subclass antibody responses to various allergens has been hampered by a lack of reliable standardized assays. The aim here was to develop quantitative immunoassays for human IgG1, IgG2, and IgG3 antibodies using ImmunoCAP® technology and to evaluate their application. METHODS: Enzyme conjugates with isotype-specific monoclonal antibodies and calibrators composed of purified myeloma paraproteins were developed for each assay and used together with other standardized assay reagents for the Phadia® 100 instrument...
February 21, 2017: International Archives of Allergy and Immunology
https://www.readbyqxmd.com/read/28208072/identification-of-triosephosphate-isomerase-as-a-novel-allergen-in-octopus-fangsiao
#4
Yang Yang, Zhong-Wei Chen, Barry K Hurlburt, Gui-Ling Li, Yong-Xia Zhang, Dan-Xia Fei, Hai-Wang Shen, Min-Jie Cao, Guang-Ming Liu
Octopus is an important mollusk in human dietary for its nutritional value, however it also causes allergic reactions in humans. Major allergens from octopus have been identified, while the knowledge of novel allergens remains poor. In the present study, a novel allergen with molecular weight of 28kDa protein was purified from octopus (Octopus fangsiao) and identified as triosephosphate isomerase (TIM) by mass spectrometry. TIM aggregated beyond 45°C, and its IgE-binding activity was affected under extreme pH conditions due to the altered secondary structure...
February 13, 2017: Molecular Immunology
https://www.readbyqxmd.com/read/28201853/antigenic-cross-reactivity-between-schistosoma-mansoni-and-peanut-a-role-for-cross-reactive-carbohydrate-determinants-ccds-and-implications-for-the-hygiene-hypothesis
#5
Joseph E Igetei, Marwa El-Faham, Susan Liddell, Michael J Doenhoff
The antigenic reactivity of constituents of Schistosoma mansoni and peanut (Arachis hypogaea) was investigated to determine whether identical antigenic epitopes possessed by both organisms provided a possible explanation for the negative correlation between chronic schistosome infection and atopy to allergens. Aqueous extracts of peanuts were probed in Western immunoblots with rabbit IgG antibodies raised against the egg, cercarial and adult worm stages of S. mansoni. Several molecules in the peanut extract were antigenically reactive with antibodies from the various rabbit anti-schistosome sera...
February 15, 2017: Immunology
https://www.readbyqxmd.com/read/28191711/bioinformatic-screening-and-detection-of-allergen-cross-reactive-ige-binding-epitopes
#6
Scott McClain
Protein allergens can be related by cross-reactivity. Allergens that share relevant sequence can cross-react, those lacking similarity in their IgE antibody-binding epitopes do not cross-react. Cross-reactivity is based on shared epitopes which is due to shared sequence and higher level structure (charge and shape). Epitopes can be important in predicting cross-reactivity potential and may provide the potential to establish criteria that identify homology among allergens. Selected allergen's IgE binding epitope sequences were used to determine how the FASTA algorithm could be used to identify a threshold of significance...
February 13, 2017: Molecular Nutrition & Food Research
https://www.readbyqxmd.com/read/28190487/measurement-of-allergen-specific-igg-in-serum-is-of-limited-value-for-the-management-of-dogs-diagnosed-with-cutaneous-adverse-food-reactions
#7
E A Hagen-Plantinga, M H G Leistra, J D Sinke, M W Vroom, H F J Savelkoul, W H Hendriks
Conflicting results have been reported in the literature in terms of the usefulness of serological testing for IgG against food allergens in dogs with cutaneous adverse food reaction (CAFR). The aim of the present study was to evaluate the suitability of a commercially available IgG ELISA for identifying food allergens in dogs, by challenging dogs with specific food ingredients, selected on the basis of IgG reactivity in serum samples. A total of 24 adult dogs with CAFR were enrolled into the study and 16 healthy dogs were included as a control group...
February 2017: Veterinary Journal
https://www.readbyqxmd.com/read/28161953/structure-of-the-major-apple-allergen-mal%C3%A2-d%C3%A2-1
#8
Linda Ahammer, Sarina Grutsch, Anna S Kamenik, Klaus R Liedl, Martin Tollinger
More than 70% of birch pollen-allergic patients develop allergic cross-reactions to the major allergen found in apple fruits (Malus domestica), the 17.5 kDa protein Mal d 1. Allergic reactions against this protein result from initial sensitization to the major allergen from birch pollen, Bet v 1. Immunologic cross-reactivity of Bet v 1-specific IgE antibodies with Mal d 1 after apple consumption can subsequently provoke severe oral allergic syndromes. This study presents the three-dimensional NMR solution structure of Mal d 1 (isoform Mal d 1...
February 15, 2017: Journal of Agricultural and Food Chemistry
https://www.readbyqxmd.com/read/28154803/involvement-of-cross-reactive-carbohydrate-determinants-specific-ige-in-pollen-allergy-testing
#9
Hidenori Yokoi, Hiroshi Yoshitake, Yuma Matsumoto, Michitsugu Kawada, Yoshiki Takato, Kiyomi Shinagawa, Hiroyuki Sakurai, Koichiro Saito
BACKGROUND: Specific IgE antibodies against the low-molecular-weight carbohydrate antigen that does not bridge IgE molecules on mast cells are not associated with clinical symptoms. Cross reactivity can be determined in allergen-specific IgE detection assays when the carbohydrate structures between pollen allergens and plant derived food allergens are similar; in such cases, false positive results for grain or legume allergens can be reported for pollen allergic patients who are not sensitized to those allergens...
January 2017: Asia Pacific Allergy
https://www.readbyqxmd.com/read/28134842/microarray-technology-applied-to-human-allergic-disease
#10
REVIEW
Robert G Hamilton
IgE antibodies serve as the gatekeeper for the release of mediators from sensitized (IgE positive) mast cells and basophils following a relevant allergen exposure which can lead to an immediate-type hypersensitivity (allergic) reaction. Purified recombinant and native allergens were combined in the 1990s with state of the art chip technology to establish the first microarray-based IgE antibody assay. Triplicate spots to over 100 allergenic molecules are immobilized on an amine-activated glass slide to form a single panel multi-allergosorbent assay...
January 28, 2017: Microarrays
https://www.readbyqxmd.com/read/28132509/comparison-of-allergenicity-at-gly-m-4-and-gly-m-bd-30k-of-soybean-after-genetic-modification
#11
Jaw-Ji Tsai, Ching-Yun Chang, En-Chih Liao
Despite rapid growth of genetically modified (GM) crops, effective evaluations of genetic modification on allergenicity are still lacking. Gly m Bd 30K is cross-reactive with cow's milk protein casein, Gly m 4, and with birch pollen allergen Bet v 1. Here we compared the allergenicity between GM and non-GM soybeans with respect to the foci Gly m 4 and Gly m Bd 30K. Recombinant allergens of Gly m Bd 30K and Gly m 4 were generated and polyclonal antibodies raised to identify these two allergenic components in soybeans...
February 7, 2017: Journal of Agricultural and Food Chemistry
https://www.readbyqxmd.com/read/28126622/purification-and-immunochemical-characterization-of-pla-l-2-the-profilin-from-plantago-lanceolata
#12
Raquel Moya, Virginia Rubio, Juan Mª Beitia, Jerónimo Carnés, M Angeles López-Matas
Profilins are small actin-binding proteins found in eukaryotes and involved in cell development, cytokinesis, membrane trafficking, and cell motility. From an allergenic point of view, profilins are panallergens usually involved in allergic polysensitization, although they are generally recognized as minor allergens. The objectives of this study were to identify and characterize the profilin from Plantago lanceolata pollen and to investigate the cross-reactivity between profilins from different pollen allergenic sources...
March 2017: Molecular Immunology
https://www.readbyqxmd.com/read/28117510/allergenicity-of-bony-and-cartilaginous-fish-molecular-and-immunological-properties
#13
REVIEW
J N Stephen, M F Sharp, T Ruethers, A Taki, D E Campbell, A L Lopata
Allergy to bony fish is common and probably increasing world-wide. The major heat-stable pan-fish allergen, parvalbumin (PV), has been identified and characterized for numerous fish species. In contrast, there are very few reports of allergic reactions to cartilaginous fish despite widespread consumption. The molecular basis for this seemingly low clinical cross-reactivity between these two fish groups has not been elucidated. PV consists of two distinct protein lineages, α and β. The α-lineage of this protein is predominant in muscle tissue of cartilaginous fish (Chondrichthyes), while β-PV is abundant in muscle tissue of bony fish (Osteichthyes)...
January 24, 2017: Clinical and Experimental Allergy: Journal of the British Society for Allergy and Clinical Immunology
https://www.readbyqxmd.com/read/28093528/a-b-cell-epitope-peptide-derived-from-the-major-grass-pollen-allergen-phl-p-1-boosts-allergen-specific-secondary-antibody-responses-without-allergen-specific-t-cell-help
#14
Meena Narayanan, Raphaela Freidl, Margarete Focke-Tejkl, Ulrike Baranyi, Thomas Wekerle, Rudolf Valenta, Birgit Linhart
More than 40% of allergic patients suffer from grass pollen allergy. Phl p 1, the major timothy grass pollen allergen, belongs to the cross-reactive group 1 grass pollen allergens that are thought to initiate allergic sensitization to grass pollen. Repeated allergen encounter boosts allergen-specific IgE production and enhances clinical sensitivity in patients. To investigate immunological mechanisms underlying the boosting of allergen-specific secondary IgE Ab responses and the allergen epitopes involved, a murine model for Phl p 1 was established...
February 15, 2017: Journal of Immunology: Official Journal of the American Association of Immunologists
https://www.readbyqxmd.com/read/28072528/triosephosphate-isomerase-and-filamin-c-share-common-epitopes-as-novel-allergens-of-procambarus-clarkii
#15
Yang Yang, Yong-Xia Zhang, Meng Liu, Soheila J Maleki, Ming-Li Zhang, Qing-Mei Liu, Min-Jie Cao, Wen-Jin Su, Guang-Ming Liu
Triosephosphate isomerase (TIM) is a key enzyme in glycolysis and has been identified as an allergen in saltwater products. In this study, TIM with a molecular mass of 28 kDa was purified from the freshwater crayfish (Procambarus clarkii) muscle. A 90-kDa protein that showed IgG/IgE cross-reactivity with TIM was purified and identified as filamin C (FLN c), which is an actin-binding protein. TIM showed similar thermal and pH stability with better digestion resistance compared with FLN c. The result of the surface plasmon resonance (SPR) experiment demonstrated the infinity of anti-TIM polyclonal antibody (pAb) to both TIM and FLN c...
February 1, 2017: Journal of Agricultural and Food Chemistry
https://www.readbyqxmd.com/read/28070926/identification-and-implication-of-an-allergenic-pr-10-protein-from-walnut-in-birch-pollen-associated-walnut-allergy
#16
Andrea Wangorsch, Annette Jamin, Jonas Lidholm, Nora Gräni, Claudia Lang, Barbara Ballmer-Weber, Stefan Vieths, Stephan Scheurer
SCOPE: English walnut (Juglans regia) belongs to the most important allergenic tree nuts. Co-sensitization with birch (Betula verrucosa) pollen has been reported. We aimed to identify a walnut allergen homologous to the major birch pollen allergen Bet v 1. METHODS AND RESULTS: A cDNA encoding a Bet v 1-homologous allergen (Jug r 5) in walnut kernels was cloned by RT-PCR. Jug r 5 was expressed in E.coli, purified by column chromatography and characterized by CD-spectroscopy...
January 9, 2017: Molecular Nutrition & Food Research
https://www.readbyqxmd.com/read/28062447/cross-react-a-new-structural-bioinformatics-method-for-predicting-allergen-cross-reactivity
#17
Surendra S Negi, Werner Braun
: The phenomenon of cross-reactivity between allergenic proteins plays an important role to understand how the immune system recognizes different antigen proteins. Allergen proteins are known to cross-react if their sequence comparison shows a high sequence identity which also implies that the proteins have a similar 3D fold. In such cases, linear sequence alignment methods are frequently used to predict cross-reactivity between allergenic proteins. However, the prediction of cross-reactivity between distantly related allergens continues to be a challenging task...
January 5, 2017: Bioinformatics
https://www.readbyqxmd.com/read/28045938/exposure-to-indoor-allergens-in-different-residential-settings-and-its-influence-on-ige-sensitization-in-a-geographically-confined-austrian-cohort
#18
Teresa Stemeseder, Bettina Schweidler, Patrick Doppler, Eva Klinglmayr, Stephanie Moser, Lisa Lueftenegger, Martin Himly, Roland Lang, Joerg Zumbach, Gertie J Oostingh, Thomas Hawranek, Arne C Bathke, Gabriele Gadermaier
BACKGROUND: Exposure to indoor allergens is crucial for IgE sensitization and development of allergic symptoms. Residential settings influence the allergen amount in house dust and hence allergic sensitization. Within this study, we investigated allergen exposure and molecule-based IgE levels in a geographically confined region and evaluated the impact of housing, pets and cleaning. METHODS: 501 adolescents from Salzburg, Austria participated in this cross-sectional study...
2017: PloS One
https://www.readbyqxmd.com/read/28039303/antigenic-determinants-of-der-p-1-specificity-and-cross-reactivity-associated-with-ige-antibody-recognition
#19
Jill Glesner, Lisa D Vailes, Caleb Schlachter, Nicholas Mank, Wladek Minor, Tomasz Osinski, Maksymilian Chruszcz, Martin D Chapman, Anna Pomés
Der p 1 and Der f 1 are major allergens from Dermatophagoides pteronyssinus and D. farinae, respectively. An analysis of antigenic determinants on both allergens was performed by site-directed mutagenesis. The analysis was based on the x-ray crystal structures of the allergens in complex with Fab fragments of three murine mAbs that interfere with IgE Ab binding: the two Der p 1-specific mAbs 5H8 and 10B9, and the cross-reactive mAb 4C1. On one hand, selected residues in the epitopes for mAb 5H8 and mAb 4C1 were substituted with amino acids that resulted in impaired Ab binding to Der p 1...
February 1, 2017: Journal of Immunology: Official Journal of the American Association of Immunologists
https://www.readbyqxmd.com/read/27997997/the-structure-of-the-mite-allergen-blo-t-1-explains-the-limited-antibody-cross-reactivity-to-der-p-1
#20
K H Meno, J S Kastrup, I-C Kuo, K Y Chua, M Gajhede
The Blomia tropicalis (Blo t) mite species is considered a storage mite in temperate climate zones and an important source of indoor allergens causing allergic asthma and rhinitis in tropical and subtropical regions. Here, we report the crystal structure of one of the allergens from Blo t, recombinant proBlo t 1 (rproBlo t 1), determined at 2.1 Å resolution. Overall, the fold of rproBlo t 1 is characteristic for the pro-form of cysteine proteases from the C1A class. Structural comparison of experimentally mapped Der f 1/Der p1 IgG epitopes to the same surface patch on Blo t 1, as well as of sequence identity of surface-exposed residues, suggests limited cross-reactivity between these allergens and Blo t 1...
December 20, 2016: Allergy
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