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Heimo Breiteneder - One of the best experts on this subject based on the ideXlab platform.
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Cross-reactivities of non-homologous allergens.
Allergy, 2020Co-Authors: Merima Bublin, Heimo BreitenederAbstract:: Allergen cross-reactivities occur when IgE antibodies, originally raised against a specific allergen, bind to identical or highly similar surface areas of another related allergen. It is a commonly held view that Cross-Reactivity requires more than 70% sequence identity, while proteins that share less than 50% sequence identity are rarely cross-reactive. This also implies that cross-reactive proteins have a similar 3D fold and belong to the same protein family. At first, the existence of Cross-Reactivity between non-homologous allergens was not expected because it was contrary to the above described concepts. Now, several lines of evidence demonstrate that IgE Cross-Reactivity also exists between unrelated allergens. In this Editorial, we aim to summarize the existing literature on IgE Cross-Reactivity between non-homologous allergens.
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Cross-Reactivity of Peanut Allergens
Current Allergy and Asthma Reports, 2014Co-Authors: Merima Bublin, Heimo BreitenederAbstract:Peanut seeds are currently widely used as source of human food ingredients in the United States of America and in European countries due to their high quality protein and oil content. This article describes the classification and molecular biology of peanut seed allergens with particular reference to their cross-reactivities. Currently, the IUIS allergen nomenclature subcommittee accepts 12 peanut allergens. Two allergens belong to the cupin and four to the prolamin superfamily, and six are distributed among profilins, Bet v 1-like proteins, oleosins, and defensins. Clinical observations frequently report an association of peanut allergy with allergies to legumes, tree nuts, seeds, fruits and pollen. Molecular Cross-Reactivity has been described between members of the Bet v 1-like proteins, the non-specific lipid transfer proteins, and the profilins. This review also addresses the less well-studied Cross-Reactivity between cupin and prolamin allergens of peanuts and of other plant food sources and the recently discovered Cross-Reactivity between peanut allergens of unrelated protein families.
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Structural bioinformatic approaches to understand Cross-Reactivity.
Molecular Nutrition & Food Research, 2006Co-Authors: Heimo Breiteneder, Clare MillsAbstract:Cross-Reactivity of allergens results from the presence of antibody-accessible conserved surface structures. These can best be studied when allergens have been structurally defined by X-ray crystallography or another structure determination method. When this is not the case, mimotope technology provides a useful alternative for elucidating antibody-binding sites on allergens. Structural bioinformatic approaches have been used to study the Cross-Reactivity of inhalant allergens with labile food allergens (Bet v 1 family) as well as the Cross-Reactivity between stable food allergens such as members of the nonspecific lipid transfer protein family. It was found that the degree of similarity of the structures correlated with the observed IgE cross-reactivities. However, IgE Cross-Reactivity between structurally unrelated allergens has not been demonstrated to date.
Rocco Luigi Valluzzi - One of the best experts on this subject based on the ideXlab platform.
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Cross-Reactivity among Beta-Lactams
Current Allergy and Asthma Reports, 2016Co-Authors: Antonino Romano, Francesco Gaeta, Maria Francisca Arribas Poves, Rocco Luigi ValluzziAbstract:Penicillins and cephalosporins are the major classes of beta-lactam (BL) antibiotics in use today and one of the most frequent causes of hypersensitivity reactions to drugs. Monobactams, carbapenems, oxacephems, and beta-lactamase inhibitors constitute the four minor classes of BLs. This review takes into account mainly the prospective studies which evaluated Cross-Reactivity among BLs in subjects with a well-demonstrated hypersensitivity to a certain class of BLs by performing allergy tests with alternative BLs and, in case of negative results, administering them. In subjects with either IgE-mediated or T-cell-mediated hypersensitivity, Cross-Reactivity among BLs, particularly among penicillins and among cephalosporins, as well as between penicillins and cephalosporins, seems to be mainly related to structural similarities among their side-chain determinants. Specifically, in penicillin-allergic subjects, Cross-Reactivity between penicillins and cephalosporins may exceed 30 % when they are administered cephalosporins with identical side chains to those of responsible penicillins. In these subjects, a few prospective studies have demonstrated a rate of Cross-Reactivity between penicillins and both carbapenems and aztreonam lower than 1 %. With regard to subjects with an IgE-mediated hypersensitivity to cephalosporins, in a single study, about 25 % of the 98 subjects with such hypersensitivity had positive results to penicillins, 3 % to aztreonam, 2 % to imipenem/cilastatin, and 1 % to meropenem. The Cross-Reactivity related to the selective recognition of the BL ring by IgE or T lymphocytes, which entails positive responses to all BLs tested, appears to be exceptional. Some studies concerning Cross-Reactivity among BLs have found patterns of allergy-test positivity which cannot be explained by either the common BL ring or by similar or identical side chains, thus indicating the possibility of coexisting sensitivities to different BLs because of prior exposures to them.
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Hypersensitivity to Aromatic Anticonvulsants: In Vivo and In Vitro Cross-Reactivity Studies
Current Pharmaceutical Design, 2006Co-Authors: Antonino Romano, Rocco Luigi Valluzzi, Rosa-maria Guéant-rodriguez, Rosa Pettinato, Maria Andriolo, Marinella Viola, Corrado Romano, Maurizio Elia, Maria Teresa Ventura, Jean-louis GuéantAbstract:Aromatic antiepileptic drugs (phenytoin, carbamazepine, oxcarbazepine, and phenobarbital) are frequently associated with cutaneous eruptions. A cell-mediated pathogenic mechanism has been demonstrated in most of such reactions on the basis of positive responses to patch tests and/or lymphocyte transformation tests. Therefore, such tests are useful tools for evaluating anticonvulsant hypersensitivity reactions. Moreover, an in vitro lymphocyte toxicity assay, which exposes the patients lymphocytes to arene oxides, has detected lymphocyte susceptibility to toxic metabolites in a large percentage of patients with hypersensitivity reactions to aromatic anticonvulsants. Although several hypersensitivity reactions to sequential exposure to more than one aromatic anticonvulsant (i.e., clinical Cross-Reactivity) have been reported, there are few studies performed with patch tests and/or lymphocyte transformation tests assessing immunologic Cross-Reactivity, and their data are contradictory. In any case, considering studies performed in samples of at least 10 patients, the immunologic Cross-Reactivity rate among aromatic anticonvulsants appears to be low. On the other hand, the reported rate of the toxic Cross-Reactivity (i.e., assessed by lymphocyte toxicity assays) is high. Further in vivo and in vitro studies in large samples of subjects are needed to evaluate Cross-Reactivity among aromatic anticonvulsants.
Wolfmeinhard Becker - One of the best experts on this subject based on the ideXlab platform.
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ubiquitous structures responsible for ige cross reactivity between tomato fruit and grass pollen allergens
The Journal of Allergy and Clinical Immunology, 1996Co-Authors: Arnd Petersen, Stefan Vieths, H Aulepp, M Schlaak, Wolfmeinhard BeckerAbstract:Abstract The simultaneous presence of IgE reactivity to tomato fruit and grass pollen allergens is evident in many patients with allergy and may be caused by Cross-Reactivity. Using sera from polysensitized patients with a positive enzyme allergosorbent test (EAST) result (score >2), we tested reactivity to both allergen sources. IgE reactivity against both extracts was demonstrated in eight serum samples, and Cross-Reactivity was confirmed by the EAST inhibition assay. The structures responsible for this Cross-Reactivity were identified by Western blotting: five of the eight sera demonstrated a 16 kd protein in both extracts, which was identified as profilin. Additionally, seven of the eight sera showed IgE binding to epitopes on carbohydrate moieties, which contained α1,3 fucosylations. To determine the allergens of tomato fruit extract, we performed two-dimensional polyacrylamide gel electrophoresis blotting. We were able to demonstrate one highly concentrated and about 20 weaker proteins possessing terminal fucose residues. These are similarly found in grass pollen extracts. It is therefore postulated that the Cross-Reactivity is affected by profilins and similar carbohydrate determinants. If carbohydrate structures can provoke IgE Cross-Reactivity between phylogenetically distant species, such structures may play an important role in sensitization and mediator release. The ubiquitous nature of the IgE-binding determinants was studied by additional EAST inhibition tests with tomato allergen disks and extract from birch pollen, mugwort pollen, apple, and celery, leading to significant inhibitions among all these allergen sources. Epitopes exclusive to grass pollen and tomato have not been detected. (J ALLERGY CLIN IMMUNOL 1996;98:805-15.)
Alfons Callebaut - One of the best experts on this subject based on the ideXlab platform.
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Cross-Reactivity of some commercially available DON and ZEN immunoaffinity columns to DON and ZEN conjugated forms and metabolites
Food Additives and Contaminants, 2011Co-Authors: Aleksandrs Versilovskis, B Huybrecht, Ek K Tangni, Sarah De Saeger, Pussemier Luc, Alfons CallebautAbstract:Abstract Seven commercially available deoxynivalenol (DON) and zearalenone (ZEN) immunoaffinity columns (IACs) were tested for Cross-Reactivity to conjugated forms (3-acetyl-deoxynivalenol, 15-acetyl-deoxynivalenol, DON-3-glucoside, DON-3-glucuronide, ZEN-glucosides, ZEN-glucuronide) and metabolites (de-epoxydeoxynivalenol, α-zearalenol, β-zearalenol) and nivalenol (NIV), using a semi-quantitative multi-mycotoxin ultra performance liquid chromatography - tandem mass spectrometry method. The DON IACs showed Cross-Reactivity for nearly all DON derivatives tested. The ZEN IACs showed limited Cross-Reactivity to some of the ZEN derivatives. The IACs were evaluated for their potential use as sample clean-up for mycotoxins in serum.
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cross reactivity of some commercially available deoxynivalenol don and zearalenone zen immunoaffinity columns to don and zen conjugated forms and metabolites
Food Additives and Contaminants Part A-chemistry Analysis Control Exposure & Risk Assessment, 2011Co-Authors: Aleksandrs Versilovskis, B Huybrecht, Ek K Tangni, Luc Pussemier, Sarah De Saeger, Alfons CallebautAbstract:Seven commercially available deoxynivalenol (DON) and zearalenone (ZEN) immunoaffinity columns (IACs) were tested for Cross-Reactivity to conjugated forms (3-acetyl-deoxynivalenol, 15-acetyl-deoxynivalenol, DON-3-glucoside, DON-3-glucuronide, ZEN-glucosides, ZEN-glucuronide) and metabolites (de-epoxydeoxynivalenol, α-zearalenol, β-zearalenol) and nivalenol (NIV), using a semi-quantitative multi-mycotoxin ultra-performance liquid chromatography-tandem mass spectrometry method. The DON IACs showed Cross-Reactivity for nearly all DON derivatives tested. The ZEN IACs showed limited Cross-Reactivity to some of the ZEN derivatives. The IACs were evaluated for their potential use as sample clean-up for mycotoxins in serum.
Anthony R. Fooks - One of the best experts on this subject based on the ideXlab platform.
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Flavivirus-induced antibody Cross-Reactivity
Journal of General Virology, 2011Co-Authors: Karen L Mansfield, Sareen E. Galbraith, Daniel L. Horton, Derek J Smith, Tom Solomon, Alan D T Barrett, Nicholas Johnson, Li Li, Anthony R. FooksAbstract:Dengue viruses (DENV) cause countless human deaths each year, whilst West Nile virus (WNV) has re-emerged as an important human pathogen. There are currently no WNV or DENV vaccines licensed for human use, yet vaccines exist against other flaviviruses. To investigate flavivirus Cross-Reactivity, sera from a human cohort with a history of vaccination against tick-borne encephalitis virus (TBEV), Japanese encephalitis virus (JEV) and yellow fever virus (YFV) were tested for antibodies by plaque reduction neutralization test. Neutralization of louping ill virus (LIV) occurred, but no significant neutralization of Murray Valley encephalitis virus was observed. Sera from some individuals vaccinated against TBEV and JEV neutralized WNV, which was enhanced by YFV vaccination in some recipients. Similarly, some individuals neutralized DENV-2, but this was not significantly influenced by YFV vaccination. Antigenic cartography techniques were used to generate a geometric illustration of the neutralization titres of selected sera against WNV, TBEV, JEV, LIV, YFV and DENV-2. This demonstrated the individual variation in antibody responses. Most sera had detectable titres against LIV and some had titres against WNV and DENV-2. Generally, LIV titres were similar to titres against TBEV, confirming the close antigenic relationship between TBEV and LIV. JEV was also antigenically closer to TBEV than WNV, using these sera. The use of sera from individuals vaccinated against multiple pathogens is unique relative to previous applications of antigenic cartography techniques. It is evident from these data that notable differences exist between amino acid sequence identity and mapped antigenic relationships within the family Flaviviridae.