Stavroula Giavi

GA2LEN skin test study II: clinical relevance of inhalant allergen sensitizations in Europe.

Background:  Skin prick testing is the standard for diagnosing IgE‐mediated allergies. A positive skin prick reaction, however, does not always correlate with clinical symptoms. A large database from a Global Asthma and Allergy European Network (GA2LEN) study with data on clinical relevance was used to determine the clinical relevance of sensitizations against the 18 most frequent inhalant allergens in Europe. The study population consisted of patients referred to one of the 17 allergy centres in 14 European countries (n = 3034, median age = 33 years). The aim of the study was to assess the clinical relevance of positive skin prick test reactions against inhalant allergens considering the predominating type of symptoms in a pan‐European population of patients presenting with suspected allergic disease.

GA2LEN skin test study III: Minimum battery of test inhalent allergens needed in epidemiological studies in patients

Background:  The number of allergens to be tested in order to identify sensitized patients is important in order to have the most cost‐effective approach in epidemiological studies.

Clinical relevance is associated with allergen-specific wheal size in skin prick testing.

Within a large prospective study, the Global Asthma and Allergy European Network (GA2LEN) has collected skin prick test (SPT) data throughout Europe to make recommendations for SPT in clinical settings.

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Wheat is an essential element in our nutrition but one of the most important food allergen sources. Wheat allergic patients often suffer from severe gastrointestinal and systemic allergic reactions after wheat ingestion. In this study, we report the molecular and immunological characterization of a new major wheat food allergen, Tri a 36. The cDNA coding for a C-terminal fragment of Tri a 36 was isolated by screening a wheat seed cDNA expression library with serum IgE from wheat food-allergic patients. Tri a 36 is a 369-aa protein with a hydrophobic 25-aa N-terminal leader peptide. According to sequence comparison it belongs to the low m.w. glutenin subunits, which can be found in a variety of cereals. The mature allergen contains an N-terminal domain, a repetitive domain that is rich in glutamine and proline residues, and three C-terminal domains with eight cysteine residues contributing to intra- and intermolecular disulfide bonds. Recombinant Tri a 36 was expressed in Escherichia coli and purified as soluble protein. It reacted with IgE Abs of ∼80% of wheat food-allergic patients, showed IgE cross-reactivity with related allergens in rye, barley, oat, spelt, and rice, and induced specific and dose-dependent basophil activation. Even after extensive in vitro gastric and duodenal digestion, Tri a 36 released distinct IgE-reactive fragments and was highly resistant against boiling. Thus, recombinant Tri a 36 is a major wheat food allergen that can be used for the molecular diagnosis of, and for the development of specific immunotherapy strategies against, wheat food allergy.

A 5-year venom immunotherapy protocol with 50 μg maintenance dose: safety and efficacy in school children

To cite this article: Konstantinou GN, Manoussakis E, Douladiris N, Hatziioannou A, Giavi S, Saxoni‐Papageorgiou P, Papadopoulos NG. A 5‐yr venom immunotherapy protocol with 50 μg maintenance dose: safety and efficacy in school children. Pediatric Allergy Immunology 2011; 22: 393–397.

The high molecular weight glutenin subunit Bx7 allergen from wheat contains repetitive IgE epitopes

Wheat is one of the most common food allergen sources for children and adults. The aim of this study was to characterize new wheat allergens using an IgE discovery approach and to investigate their IgE epitopes.

Oral immunotherapy with low allergenic hydrolysed egg in egg allergic children

A major drawback of oral immunotherapy for food allergy is the possibility of severe side‐effects. We assessed both safety and efficacy of a low allergenic hydrolysed egg (HydE) preparation used in a double‐blind placebo‐controlled randomized study in egg allergic children.

Cow’s milk allergy as a cause of anaphylaxis to systemic corticosteroids

unblinded manner. Six to ten hours after consumption of kiwi she reproducibly developed an itchy rash consisting of confluent 3–5 mm purpuric macules and papules on the legs, lower trunk and forearms with consecutive bleeding in the central part of the lesions. Oral provocations with apple, banana and pineapple were negative. Western Blot analysis of a kiwi fruit extract with the patient’s serum showed IgG-, but no IgE-reactivity, corresponding to themajor kiwi fruit antigen Act c 1 (Fig. 1C). HE staining of a fresh lesion, that was taken soon after appearance, showed neutrophilic infiltration in and around cutaneous vessels with leucocytoclasia consistent with leucocytoclastic (allergic) vasculitis (Fig. 1D/E). In the light of the patient’s history, diagnostic findings and the reproducible induction of symptoms by oral provocation with kiwi, we diagnosed ‘kiwiinduced allergic leucocytoclastic vasculitis’. Elimination diet with avoidance of the consumption of kiwi lead to slow resolution of the purpuric lesions and hyperpigmentations over time. No recurrences of vasculitis were observed over a period of 3 years. Using repeated oral food challenges we were able to identify kiwi fruits as a causal elicitor of allergic vasculitis. The presence of Act c 1-specific IgG strongly supports an antigen-specific process, but food-specific IgG antibodies are also frequent finding in healthy individuals (1). Foodstuff is rarely considered as a cause for allergic vasculitis in clinical practice and is reported only anecdotally in current literature (rye, carrot, cow’s milk, hen’s egg, cocoa products and additives) (2–4). Strikingly, in our patient mainly dependent body regions like legs and feet were affected by vasculitis and therefore, the formation of IgG immune complexes with kiwi antigen and their deposition in dermal postcapillary venules can be assumed as pathogenic process (5). The authors report no conflict of interest. J.G., S.K., and J.R. cared for the patient. J.G. and S.K. wrote the manuscript. M.O., M.M. and J.R. reviewed the manuscript. M.O. performed the western blot.

Risk of allergic reactions to wine, in milk, egg and fish-allergic patients.

BackgroundEuropean legislators and wine producers still debate on the requirement for labeling of wines fined with potentially allergenic food proteins (casein, egg white or fish-derived isinglass). We investigated whether wines fined with known concentrations of these proteins have the potential to provoke clinical allergic reactions in relevant patients.MethodsIn-house wines were produced for the study, fined with different concentrations of casein (n = 7), egg albumin (n = 1) and isinglass (n = 3). ELISA and PCR kits specific for the respective proteins were used to identify the fining agents. Skin prick tests and basophil activation tests were performed in patients with confirmed IgE-mediated relevant food allergies (n = 24). A wine consumption questionnaire and detailed history on possible reactions to wine was obtained in a multinational cohort of milk, egg or fish allergic patients (n = 53) and patients allergic to irrelevant foods as controls (n = 13).ResultsFining agents were not detectable in wines with the available laboratory methods. Nevertheless, positive skin prick test reactions and basophil activation to the relevant wines were observed in the majority of patients with allergy to milk, egg or fish, correlating with the concentration of the fining agent. Among patients consuming wine, reported reactions were few and mild and similar with the ones reported from the control group.ConclusionCasein, isinglass or egg, remaining in traces in wine after fining, present a very low risk for the respective food allergic consumers. Physician and patient awareness campaigns may be more suitable than generalized labeling to address this issue, as the latter may have negative impact on both non-allergic and allergic consumers.

Heating does not decrease immunogenicity of goat's and ewe's milk

URE 1. A, SDS-PAGE (A-1) and Western blot analysis (A-2) with u , and EM allergies and milk-tolerant negative control showed high an d (A-3). ALA, a-Lactalbumin; BLG, b-lactoglobulin; CC, cow’s che ecular weight; SA, serum albumin. extensive amino acid sequence identity of milk proteins (85%100%; see Tables E1 and E2 in this article’s Online Repository at www.jaci-inpractice.org) and similar proteome profiles that imply similarity of protein functions. However, selective GM and ewe’s milk (EM) allergy without CMA (GEMA) have been reported, including anaphylaxis to cheeses from GM and EM in CM-tolerant children. GEMA implies existence of unique GM and EM-allergenic epitopes that are different from CMallergenic epitopes. Among children with CMA, >70% can tolerate extensively heated CM in baked products. We sought to determine the effects of heating on the immunogenicity of GM and EM proteins in children with GEMA. We recruited 17 subjects with milk allergy from Spain, Greece, and the United States; 13 were males; median age was 7.2 years, and 25% to 75% interquartile range (IQR) was 4.0 to 9.9 years. The study was approved by the Institutional Review Boards at The Mount Sinai School of Medicine, Pediatric Hospital “P & A Kiriakou,” and Hospital Infantil Universitario Nino Jesus; informed consent was obtained from the subjects. Eight subjects with CM allergy tolerated extensively heated oral milk challenge but reacted to unheated milk challenge. Nine subjects had history of convincing, immediate allergic symptoms on ingestion of GM or EM or both (Table I). The 8