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Background Hymenoptera stings can cause severe anaphylaxis in untreated venom-allergic patients. A correct diagnosis regarding the relevant species for immunotherapy is often hampered by clinically irrelevant cross-reactivity. In vespid venom allergy, cross-reactivity between venoms of different species can be a diagnostic challenge. To address immunological IgE cross-reactivity on molecular level, seven recombinant antigens 5 of the most important Vespoidea groups were assessed by different diagnostic setups. Methods The antigens 5 of yellow jackets, hornets, European and American paper wasps, fire ants, white-faced hornets, and Polybia wasps were recombinantly produced in insect cells, immunologically and structurally characterized, and their sIgE reactivity assessed by Immuno CAP, ELISA, cross-inhibition, and basophil activation test ( BAT) in patients with yellow jacket or Polistes venom allergy of two European geographical areas. Results All recombinant allergens were correctly folded and structural models and patient reactivity profiles suggested the presence of conserved and unique B-cell epitopes. All antigens 5 showed extensive cross-reactivity in sIgE analyses, inhibition assays, and BAT. This cross-reactivity was more pronounced in Immuno CAP measurements with venom extracts than in sIgE analyses with recombinant antigens 5. Dose-response curves with the allergens in BAT allowed a differentiated individual dissection of relevant sensitization. Conclusions Due to extensive cross-reactivity in various diagnostic settings, antigens 5 are inappropriate markers for differential sIgE diagnostics in vespid venom allergy. However, the newly available antigens 5 from further vespid species and the combination of recombinant allergen-based sIgE measurements with BAT represents a practicable way to diagnose clinically relevant sensitization in vespid venom allergy. [ABSTRACT FROM AUTHOR]

W. K. Yong and D. D. Heath published in 1979 a seminal paper in the first issue of Parasite Immunology describing their efforts to determine whether the arc 5 precipitin band, formed when test human serum is reacted against electrophoresed hydatid cyst fluid antigen, would be a suitable immunodiagnostic test for the identification of sheep infected with Echinococcus granulosus. Although they found antibodies to arc 5 in the sera of hydatid-infected sheep, the sera of some sheep harbouring Taenia ovis and T. hydatigena also precipitated the hydatid cyst fluid arc 5 antigen, so they concluded arc 5 antibodies were not suitable for the specific immunodiagnosis of E. granulosus infection in sheep in New Zealand. Subsequent work has shown that the existence of multiple infections with different taeniid species, antigenic cross-reactivity between these related parasites and the low level of specific antibody response to infection continue to hinder efforts to improve the diagnosis of hydatid infection in sheep and other natural intermediate hosts, thereby preventing the development of any practical test. In particular, the poor antibody response of ruminants to naturally acquired hydatid infection may prove an insurmountable barrier in future efforts to develop a reliable and accurate immunological test. [ABSTRACT FROM AUTHOR]

BACKGROUND: Snail allergy is rare but can be fatal. Pila polita, a freshwater snail, was considered as a popular exotic food, particularly in tropical countries, and consumed in processed forms. Thus, the purpose of this study was to identify the major and cross‐reactive allergens of P. polita and to determine the impact of food processing on the allergen stability. RESULTS: Sodium dodecyl sulfate–polyacrylamide gel electrophoresis fractionated raw snail extract to approximately 24 protein bands, between 9 and 245 kDa. The prominent band at 33 kDa was detected in all raw and processed snail extracts. Immunoblotting tests of the raw extract demonstrated 19 immunoglobulin E (IgE)‐binding proteins, and four of them, at 30, 35, 42 and 49 kDa, were revealed as the major IgE‐binding proteins of P. polita. Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry identified the 49 and 42 kDa major allergens as actin, whereas the 30 and 35 kDa major allergens were identified as tropomyosin. Immunoblotting revealed that the raw snail had more allergenic proteins than the processed snail. The degree of allergenicity in decreasing order was raw > brine pickled> boiled > roasted > fried > vinegar pickled. The presence of cross‐reactivity between P. polita and the shellfish tested was exhibited with either no, complete, or partial inhibitions. CONCLUSION: Actin and tropomyosin were identified as the major and cross‐reactive allergens of P. polita among local patients with snail allergy. Those major allergens are highly stable to high temperatures, acidic pH, and high salt, which might played a crucial role in snail allergy in Malaysia. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Background: Allergy to celery is often associated with sensitization to birch and;or mugwort pollen. Objective and Methods: In a multi-centre study. sera from 23 patients suffering from type I allergy to celery and 1 5 patients with positive celery RAST hut no clinical sensitization were compared. To examine whether cross-reactivity between celery and mugwort pollen includes cross-sensitization to birch pollen allergens, we determined cross-reacting structure in birch pollen. mugwort pollen and celery by means of immunoblotting. Inhibition studies were performed by preincubation of sent with extracts of birch pollen. mugwort pollen, and celery. Results: We identified three groups of proteins homologues of Bet v 1 and birch profilin (Bet v2) as well as a group of proteins with a molecular range of 46 to 60KD displaying IgE-cross-reactivity. which were shared by birch pollen and celery. Two of these groups of allergens (profilin and the 46 to 60 U) proteins) were also present in mugwort pollen. In this paper we demonstrate that most cross-reacting allergens present in mugwort pollen and celery can also be detected in birch pollen extract. Conclusion therefore we propose. Iron a serological point of view, to extend the mugwort-celery syndrome to the birch-mugwort-celery syndrome. [ABSTRACT FROM AUTHOR]

p-phenylenediamine derivatives are widely used in industry and in cosmetics, and several of them are well-known sensitizers. One group of allergenic p-phenylenediamine derivatives are used as colour film developers. Cross-reactivity between the colour film developers has been reported. In this paper, an occupational facial dermatitis due to colour film developers is described. The patient reacted to colour film developers (CD-1, CD-2, CD-3. and CD-4), but not to other p-phenylenediamine derivatives tested. He also showed allergic reactions to Disperse Blue 106 and Disperse Blue 124 and to Disperse Red 17, but not to Disperse Orange 3. The activation of the colour him developers by oxidation at physiological pH was analysed with chemical methods, and the mechanism responsible tar the concomitant reactivities to the colour film developers and the disperse dyes at a molecular level is discussed. [ABSTRACT FROM AUTHOR]

Nonsteroidal anti‐inflammatory drugs (NSAIDs) are among the main causes of fixed drug eruption (FDE). Cross‐sensitivity between chemically unrelated NSAIDs has been rarely described in FDE. We report herein two cases of NSAID‐induced FDE confirmed by oral provocation test (OPT) with a literature review. Case 1 is a 49‐year‐old woman who took mefenamic, naproxen and acetaminophen for lumbago. On the second day, she noticed three erythematous plaques, located in the upper lip, chin and the right hand, which faded spontaneously, leaving residual patches. Three months later, she took mefenamic acid with reactivation of the same plaques. She received naproxen. On the same day, she exhibited a reactivation of lesions with the development of a new one. These lesions have disappeared leaving hyperpigmented sequelae. After negative patch test to naproxen, an OPT was performed with positive reaction, observed on the third day. To establish the cross‐reactivity, she underwent OPTs, which gave positive results to indomethacin, ketoprofen and tiaprofenic acid. Case 2 is a 52‐year‐old woman who presented painful dusky‐red macules, located in the right and left wrists, 24 hours after taking mefenamic acid. She described two similar events that occurred in the past with an undefined drug and piroxicam. Patch tests to lysine acetylsalicylate, mefenamic acid, piroxicam, naproxen and celecoxib were negative. OPTs to the same NSAIDs gave positive results to lysine acetylsalicylate, piroxicam and mefenamic acid. Thirteen case reports, seven case series and one retrospective analysis, including cases with confirmed cross‐reactivity between NSAIDs, were reported in literature. Clinicians should be aware of such phenomenon. [ABSTRACT FROM AUTHOR]

Drug reaction with eosinophilia and systemic symptom (DRESS) is a severe adverse drug‐induced reaction. Commonly related to anticonvulsant and allopurinol, DRESS can affect both adults and children. Cefotaxime is rarely associated with DRESS, especially with children. We report a cefotaxime‐induced DRESS in a child and emphasize the role of allergological work‐up to point out the culprit drug in exploring cross‐reactivity and identifying a possible cosensitization. A 2‐year‐old boy was treated with cefotaxime, vancomycin and metronidazole for acute otomastoiditis. Metronidazole was withdrawn and vancomycin was changed by teicoplanin 10 and 15 days later, respectively. Nineteen days after ongoing cefotaxime and 4 days after teicoplanin intake, the patient developed hyperthermia, a widespread exanthema, facial oedema with neither mucosal involvement nor palpable lymphadenopathy. Biological tests revealed eosinophilia, atypical lymphocytes, mild cytolysis and a high lactate dehydrogenase level. Serological tests for viral and bacterial infections were negative. DRESS was suspected and the 2 antibiotics were withdrawn. Intradermal tests (IDT) were carried out 2 months later with cefotaxime and teicoplanin. They revealed a positive result at 48‐hour reading. To assess cross‐reactivity among β‐lactams, IDT to penicillins (benzylpenicillin, amoxicillin and oxacillin) was performed showing negative results at 48‐hour reading. Nevertheless, IDT to cephalosporins (cefazolin, cefuroxime, ceftazidime and ceftriaxone) displayed positive results at 48‐hour reading. As a result, IDT are of great interest and should be performed to confirm the role of cefotaxime and detect a potential cross‐reactivity with chemically similar drugs and drugs taken before and during the episode of DRESS. [ABSTRACT FROM AUTHOR]

Electrochemical biosensors based on structure‐switching aptamers offer many advantages because they can operate directly in complex samples and offer the potential to integrate with miniaturized electronics. Unfortunately, these biosensors often suffer from cross‐reactivity problems when measuring a target in samples containing other chemically similar molecules, such as precursors or metabolites. While some progress has been made in selecting highly specific aptamers, the discovery of these reagents remains slow and costly. In this work, a novel strategy is demonstrated to distinguish molecules with miniscule difference in chemical composition (such as a single hydroxyl group)—with cross reactive aptamer probes—by tuning the charge state of the surface on which the aptamer probes are immobilized. As an exemplar, it is shown that the strategy can distinguish between DOX and many structurally similar analytes, including its primary metabolite doxorubicinol (DOXol). Then the ability to accurately quantify mixtures of these two molecules based on their differential response to sensors with different surface‐charge properties is demonstrated. It is believed that this methodology is general and can be extended to a broad range of applications. [ABSTRACT FROM AUTHOR]

Background: Although avian coronavirus infectious bronchitis virus (IBV) and SARS‐CoV‐2 belong to different genera of the Coronaviridae family, exposure to IBV may result in the development of cross‐reactive antibodies to SARS‐CoV‐2 due to homologous epitopes. We aimed to investigate whether antibody responses to IBV cross‐react with SARS‐CoV‐2 in poultry farm personnel who are occupationally exposed to aerosolized IBV vaccines. Methods: We analyzed sera from poultry farm personnel, COVID‐19 patients, and pre‐pandemic controls. IgG levels against the SARS‐CoV‐2 antigens S1, RBD, S2, and N and peptides corresponding to the SARS‐CoV‐2 ORF3a, N, and S proteins as well as whole virus antigens of the four major S1‐genotypes 4/91, IS/1494/06, M41, and D274 of IBV were investigated by in‐house ELISAs. Moreover, live‐virus neutralization test (VNT) was performed. Results: A subgroup of poultry farm personnel showed elevated levels of specific IgG for all tested SARS‐CoV‐2 antigens compared with pre‐pandemic controls. Moreover, poultry farm personnel, COVID‐19 patients, and pre‐pandemic controls showed specific IgG antibodies against IBV strains. These antibody titers were higher in long‐term vaccine implementers. We observed a strong correlation between IBV‐specific IgG and SARS‐CoV‐2 S1‐, RBD‐, S2‐, and N‐specific IgG in poultry farm personnel compared with pre‐pandemic controls and COVID‐19 patients. However, no neutralization was observed for these cross‐reactive antibodies from poultry farm personnel using the VNT. Conclusion: We report here for the first time the detection of cross‐reactive IgG antibodies against SARS‐CoV‐2 antigens in humans exposed to IBV vaccines. These findings may be useful for further studies on the adaptive immunity against COVID‐19. [ABSTRACT FROM AUTHOR]

Background: Insights into the IgE cross‐sensitization and possible cross‐reactivity patterns of sera reactive to chlorhexidine (CHX) are still incomplete and are likely to benefit from a functional exploration using a passive mast cell activation test (pMAT). Therefore, we want to study whether the pMAT with CHX‐specific IgE (sIgE) enables to depict effector cell degranulation in response to alexidine (ALX), octenidine (OCT) and/or polyhexamethylene biguanide (PHMB) indicative of cross‐reactivity between these compounds and CHX. Methods: Serum of 10 CHX‐allergic patients, nine individuals with an isolated sIgE CHX and five healthy controls were included. Human cultured mast cells (MCs) were, before and after sensitization, challenged with CHX, ALX, OCT or PHMB. Degranulation was measured via quantification of upregulation of CD63. Results: Mast cell responsiveness to ALX and OCT was demonstrable with 4/10 and 3/10 of the sera of CHX‐allergic patients respectively. Percentage of degranulation varied between 12 and 34% for ALX‐reactive MCs and between 4 and 22% for OCT‐reactive MCs. No reactivity to ALX or OCT was demonstrable when using sera obtained from individuals with an isolated sIgE CHX or from healthy controls. Unlike CHX, ALX and OCT, PHMB turned out to be a direct MC activator via occupation of MRGPRX2. PHMB‐reactive sIgEs were demonstrable in some patients with an isolated sIgE CHX but were unable to trigger PHMB‐induced degranulation in MRGPRX2 knockdown MCs. Conclusion: Mast cells constitute an attractive tool to explore cross‐reactivity between structurally similar compounds. Along with the identification of safe alternatives for the individual patient, the pMAT can advance our insights into sIgE cross‐reactivity patterns including assessment of molecules not yet approved for human use. [ABSTRACT FROM AUTHOR]

Background: Several studies have reported in vitro cross‐reactivity between wheat and barley. However, evidence regarding the clinical cross‐reactivity of wheat and barley is limited. This study examined the clinical cross‐reactivity of barley and wheat among children with immediate‐type wheat allergies. Methods: We examined the threshold dose of a wheat oral food challenge for wheat‐allergic children. We examined the reactivity of barley, and the oral food challenges of barley tea and barley rice were implemented as needed. We measured the specific immunoglobulin E (sIgE) levels in wheat, ω‐5 gliadin, and barley. Results: We evaluated 53 children (39 [74%] boys) with a median age of 6.6 years. Among them, 39 (74%) patients had a history of anaphylaxis to wheat. The median wheat‐, barley‐, and ω‐5 gliadin‐sIgE levels were 57.3, 12.1, and 3.2 kUA/L, respectively. Twelve patients reacted to barley tea (1.8 mg), 14 reacted to barley rice (220–440 mg), and 27 were tolerant to barley tea and barley rice. Barley‐allergic patients had significantly higher wheat‐ and ω‐5 gliadin‐ and barley‐sIgE levels and significantly lower threshold doses of wheat than barley‐tolerant patients. Omega‐5 gliadin‐sIgE was the most useful predictor of barley allergy among wheat‐allergic patients; the ω‐5 gliadin‐sIgE 95% positive predictive value for barley allergy was 4.6 kUA/L. Conclusions: Half of wheat‐allergic children reacted to barley. A lower threshold dose of wheat is related to cross‐reactive barley allergies. Omega‐5 gliadin‐sIgE predicts cross‐reactive barley allergy in children allergic to wheat. Clinical cross‐reactivity to barley should be considered in the management of wheat‐allergic children. [ABSTRACT FROM AUTHOR]

Background: Oral immunotherapy (OIT) is a treatment option for patients with milk, egg, and peanut allergy, but data on the efficacy and safety of cashew OIT are limited. Methods: A cohort of 50 cashew‐allergic patients aged ≥4 years, who were consecutively enrolled into cashew OIT (target dose 4000 mg protein) between 4/2016 and 12/2019. Fifteen cashew‐allergic patients who continued cashew elimination served as observational controls. Co‐allergy to pistachio and walnut was determined. Full desensitization rate and associated immunological changes in both groups were compared. Patients fully desensitized to cashew were instructed to consume a dose of 1200 mg cashew protein for 6 months and were then challenged to a full dose. Patients with co‐allergy to pistachio or walnut were challenged to the respective nut. Results: Forty‐four of 50 OIT‐treated patients (88%) compared to 0% in controls tolerated a dose of 4000 mg cashew protein at the end of the study (odds ratio 8.3, 95% CI 3.9–17.7, p < 0.001). An additional three patients were desensitized to 1200 mg cashew protein, and three patients stopped treatment. Three patients (6%) were treated with injectable epinephrine for home reactions. Desensitized patients had decreased SPT, sIgE, basophil reactivity, and increased sIgG4, following treatment. Following cashew desensitization, all pistachio (n = 35) and four of eight walnut co‐allergic patients were cross‐desensitized to the respective nut. All (n = 44) patients consuming a low cashew dose for ≥6 months following desensitization passed a full‐dose cashew OFC. Conclusions: Cashew OIT desensitizes most cashew‐allergic patients and cross‐desensitizes to pistachio. Safety is similar to OIT for other foods. [ABSTRACT FROM AUTHOR]

Sensitization to lipid transfer protein (LTP), the most frequent cause of food allergy in southern Europe, still shows several controversial, but also intriguing, aspects. Some of these include the degree of cross‐reactivity between LTPs from botanically distant sources, the definition of risk factors, the role of some cofactors, clinical outcomes, geographical differences and the identification of the primary sensitizer in different areas. This review article tries to analyse and comment on these aspects point by point suggesting some explanatory hypotheses with the final scope to stimulate critical thoughts and elicit the scientific discussion about this issue in the readership. [ABSTRACT FROM AUTHOR]

The American Polistes species venom mixture – that of P. annularis, P. fuscatus, P. metricus and P. exclamans– was the only commercially available mixture for diagnosis and therapy until 1996. However, these species of Polistes are not present in Europe, where P. dominulus and P. gallicus and to a lesser extent P. nimphus are widespread. The aim of this study was to assess the allergenic differences among the commercial American mix, P. dominulus and P. gallicus venom in European patients and therefore to verify if this mixture is suitable for diagnosis in these patients. We carried out skin tests, radioallergosorbent tests (RAST) and RAST inhibition in Italian patients with adverse reactions to Polistes stings. RAST inhibition results demonstrated that cross-reactivity between the American and European species is only partial and that P. dominulus and P. gallicus venoms have exclusive allergens. Skin tests and direct RAST confirmed these results and also showed that European Polistes venom is more suitable than the American mix in Italian patients. Moreover, we found a high rate of cross-reactivity between P. dominulus and P. gallicus. To conclude, P. dominulus and/or P. gallicus venoms are necessary for diagnosis and therefore in the therapy of European patients. [ABSTRACT FROM AUTHOR]

Background and Objective Due to the increasing popularity of exotic fruits in the Western diet, allergologists are confronted with allergic reactions to substances in these plants. The present report describes an anaphylactic reaction after the consumption of lychee fruit (Litchi sinensis). The atopic patient also suffers from rhinoconjunctivitis due to a sensitization against pollen of the Compositae family, as well as from dyspnoea after eating sunflower seeds. Our goals were to determine crossreactivity between antibodies against lychee fruit and other plants and to characterize the allergen. Methods and results Specific IgE against lychee fruits were detected by an EAST assay. The allergen was characterized by immunoblot, immunoblot inhibition and EAST inhibition assays. Broad crossreactivity between lychee fruit and other plants was found and profilin identified as the protein responsible for the patient s complex allergy syndrome. Conclusion Lychee fruit contains a significant amount of profilin. Consumption of this exotic fruit can cause severe anaphylactic reactions in patients being sensitized against the plant pan-allergen profilin. [ABSTRACT FROM AUTHOR]

Enterobacteriaceae are a large family of Gram‐negative bacteria that includes both commensals and opportunistic pathogens. The latter can cause severe nosocomial infections, with outbreaks of multi‐antibiotics resistant strains, thus being a major public health threat. In this study, we report that Enterobacteriaceae‐reactive memory Th cells were highly enriched in a CCR6+CXCR3+ Th1*/17 cell subset and produced IFN‐γ, IL‐17A, and IL‐22. This T cell subset was severely reduced in septic patients with K. pneumoniae bloodstream infection who also selectively lacked circulating K. pneumonie‐reactive T cells. By combining heterologous antigenic stimulation, single cell cloning and TCR Vβ sequencing, we demonstrate that a large fraction of memory Th cell clones was broadly cross‐reactive to several Enterobacteriaceae species. These cross‐reactive Th cell clones were expanded in vivo and a large fraction of them recognized the conserved outer membrane protein A antigen. Interestingly, Enterobacteriaceae broadly cross‐reactive T cells were also prominent among in vitro primed naïve T cells. Collectively, these data point to the existence of immunodominant T cell epitopes shared among different Enterobacteriaceae species and targeted by cross‐reactive T cells that are readily found in the pre‐immune repertoire and are clonally expanded in the memory repertoire. [ABSTRACT FROM AUTHOR]

Objectives: The emergence of a SARS‐CoV‐2 variant with a point mutation in the spike (S) protein, D614G, has taken precedence over the original Wuhan isolate by May 2020. With an increased infection and transmission rate, it is imperative to determine whether antibodies induced against the D614 isolate may cross‐neutralise against the G614 variant. Methods: Antibody profiling against the SARS‐CoV‐2 S protein of the D614 variant by flow cytometry and assessment of neutralising antibody titres using pseudotyped lentiviruses expressing the SARS‐CoV‐2 S protein of either the D614 or G614 variant tagged with a luciferase reporter were performed on plasma samples from COVID‐19 patients with known D614G status (n = 44 infected with D614, n = 6 infected with G614, n = 7 containing all other clades: O, S, L, V, G, GH or GR). Results: Profiling of the anti‐SARS‐CoV‐2 humoral immunity reveals similar neutralisation profiles against both S protein variants, albeit waning neutralising antibody capacity at the later phase of infection. Of clinical importance, patients infected with either the D614 or G614 clade elicited a similar degree of neutralisation against both pseudoviruses, suggesting that the D614G mutation does not impact the neutralisation capacity of the elicited antibodies. Conclusions: Cross‐reactivity occurs at the functional level of the humoral response on both the S protein variants, which suggests that existing serological assays will be able to detect both D614 and G614 clades of SARS‐CoV‐2. More importantly, there should be negligible impact towards the efficacy of antibody‐based therapies and vaccines that are currently being developed. [ABSTRACT FROM AUTHOR]

(B) D2: strong positive patch test reactions (++) to sesquiterpene lactone mix (SLM) 0.1% pet. on the previous positive patch tests sites of IBOA (no. 1 = 0.1%, no. 2 = 0.3%) on the right upper arm. Keywords: allergic contact dermatitis; case report; cosensitization; cross-reactivity; diabetes mellitus; FreeStyle Libre; glucose sensor; medical devices; re-test method; sesquiterpene lactones EN allergic contact dermatitis case report cosensitization cross-reactivity diabetes mellitus FreeStyle Libre glucose sensor medical devices re-test method sesquiterpene lactones 57 59 3 12/17/21 20220101 NES 220101 Patients with allergic contact dermatitis from the glucose sensor FreeStyle Libre (Abbott Diabetes Care, Witney, UK) are often (strongly) sensitized to isobornyl acrylate (IBOA).1,2 About 40% to 60% of these patients also have a concomitant positive patch test to the sesquiterpene lactone mix (SLM; 0.1% pet.), Unexpected positive patch test reactions to sesquiterpene lactones in patients sensitized to the glucose sensor FreeStyle libre. [Extracted from the article]

Background: Analysis of cross-reactivity is necessary for prescribing safe cephalosporins for penicillin allergic patients. Amoxicillin (AX) is the betalactam most often involved in immediate hypersensitivity reactions (IHRs), and cefadroxil (CX) the most likely cephalosporin to cross-react with AX, since they share the same R1 side chain, unlike cefuroxime (CO), with a structurally different R1. We aimed to analyse cross-reactivity with CX and CO in patients with confirmed IHRs to AX, including sIgE recognition to AX, CX, CO, and novel synthetic determinants of CX. Methods: Fifty-four patients with confirmed IHRs to AX based on skin test (ST) and/or drug provocation test (DPT) were included. Serum sIgE to AX and benzylpenicillin was determined by Radioallergosorbent test (RAST). Two potential determinants of CX, involving intact or modified R1 structure, with open betalactam ring, were synthesised and sIgE evaluated by RAST inhibition assay. Results: Tolerance to CX (Group A) was observed in 64.8% cases and cross-reactivity in 35.2% cases (Group B). Cross-reactivity with CO was only found in 1.8% cases from Group B. ST to CX showed a negative predictive value of 94.6%. RAST inhibition assays showed higher recognition to CX as well as to both synthetic determinants (66% of positive cases) in Group B. Conclusions: Cross-reactivity with CX in AX allergic patients is 35%, being ST not enough for prediction. R1, although critical for recognition, is not the unique factor. The synthetic determinants of CX, 1-(HOPhG-Ser-Bu) and 2-(pyrazinone) are promising tools for determining in vitro cross-reactivity to CX in AX allergic patients. [ABSTRACT FROM AUTHOR]

The article presents a case report of contact urticaria and dermatitis induced by Solanaceae and Alliaceae in a 48-year-old female supermarket manager. The paper provides information on the patient's medical history, clinical presentation of the disease, results of medical examinations and treatment and management of the disease.

Background: Ole e 7 is a nonspecific lipid transfer protein (nsLTP) from olive pollen, one of the main allergenic pollens worldwide. This allergenic nsLTP is responsible for severe symptoms in regions with high olive pollen exposure, where many Ole e 7‐sensitized patients exhibit a co‐sensitization to the peach nsLTP, Pru p 3. However, there is no evidence of cross‐reactivity, which explains this observed co‐sensitization. Therefore, the purpose of this study was to explore the relationship between Ole e 7 and Pru p 3. Methods: A total of 48 patients sensitized to Ole e 7 and/or Pru p 3 were included in the study. Specific IgE serum levels were measured by ImmunoCAP 250 and ELISA. Inhibition assays were performed to determine the existence of cross‐reactivity between both nsLTPs. Allergic response was analyzed ex vivo (basophil activation test) and in vitro (RBL‐2H3 mast cell model). Results: Common IgG and IgE epitopes were identified between both allergens. IgE‐binding inhibition was detected in Ole e 7–monosensitized patients using rPru p 3 as inhibitor, reaching inhibition values of 25 and 100%. Ex vivo and in vitro assays revealed a response against rPru p 3 in four (31%) Ole e 7–monosensitized patients. Conclusions: Our results suggest that Ole e 7 could play a new role as primary sensitizer in regions with high olive pollen exposure, leading to the peach nsLTP sensitization. This co‐sensitization process would occur because of the cross‐reactivity between Ole e 7 and Pru p 3 observed in some allergic patients. [ABSTRACT FROM AUTHOR]

Background and aims: Recent studies have found an increase in the seroprevalence of hepatitis E virus (HEV) infection in patients with autoimmune hepatitis (AIH). We aimed to assess the prevalence of positive anti‐HEV IgM and IgG, and HEV‐RNA in a cohort of patients with AIH, to determine the impact of positive HEV serology on patient outcome, and to evaluate the role of hypergammaglobulinemia and positive autoantibodies in the presence of positive anti‐HEV serology. Methods: One hundred and five patients tested for HEV infection between 2014 and 2018 were included in the study: 50 with chronic AIH (more than 1 year on treatment), and 55 with an acute hepatitis (30 patients with acute AIH and 25 with non‐AIH). Results: Seroprevalence of HEV was higher in patients with acute AIH (17% vs 10% in patients with chronic AIH and 8% in patients with non‐AIH). Patients with acute AIH and positive anti‐HEV IgG were older (58 vs 40; P =.006), had higher IgG levels (27 g/dL vs 13 g/dL; P =.03) and antismooth muscle antibodies (ASMA) titres (1:160 vs 1:80; P =.045), and were more likely to have another autoimmune disease (60% vs 16%; P =.03). At the time of HEV testing, anti‐HEV IgG positive patients had significantly higher serum IgG levels (17 g/L vs 11 g/L; P =.009), ANA (1:160 vs 1:60; P =.026) and ASMA titres (1:80 vs 1:40; P =.021). Conclusion: Seroprevalence of HEV in patients with AIH in Catalonia does not differ from that of the general population. The higher HEV seroprevalence in patients with acute AIH with higher levels of gammaglobulins and high antibody titres suggest the presence of cross‐reactivity between HEV and liver antigens. [ABSTRACT FROM AUTHOR]

Background: Analysis of cross‐reactivity is necessary for prescribing safe cephalosporins for penicillin allergic patients. Amoxicillin (AX) is the betalactam most often involved in immediate hypersensitivity reactions (IHRs), and cefadroxil (CX) the most likely cephalosporin to cross‐react with AX, since they share the same R1 side chain, unlike cefuroxime (CO), with a structurally different R1. We aimed to analyse cross‐reactivity with CX and CO in patients with confirmed IHRs to AX, including sIgE recognition to AX, CX, CO, and novel synthetic determinants of CX. Methods: Fifty‐four patients with confirmed IHRs to AX based on skin test (ST) and/or drug provocation test (DPT) were included. Serum sIgE to AX and benzylpenicillin was determined by Radioallergosorbent test (RAST). Two potential determinants of CX, involving intact or modified R1 structure, with open betalactam ring, were synthesised and sIgE evaluated by RAST inhibition assay. Results: Tolerance to CX (Group A) was observed in 64.8% cases and cross‐reactivity in 35.2% cases (Group B). Cross‐reactivity with CO was only found in 1.8% cases from Group B. ST to CX showed a negative predictive value of 94.6%. RAST inhibition assays showed higher recognition to CX as well as to both synthetic determinants (66% of positive cases) in Group B. Conclusions: Cross‐reactivity with CX in AX allergic patients is 35%, being ST not enough for prediction. R1, although critical for recognition, is not the unique factor. The synthetic determinants of CX, 1 ‐(HOPhG‐Ser‐Bu) and 2 ‐(pyrazinone) are promising tools for determining in vitro cross‐reactivity to CX in AX allergic patients. [ABSTRACT FROM AUTHOR]

Abstract: Background: Profilins are dominant pan‐allergens known to cause cross‐sensitization, leading to clinical symptoms such as pollen‐food syndrome. This study aimed to determine the T‐cell response to Phl p 12 in profilin‐sensitized patients, by measuring the prevalence, strength and cross‐reactivity to clinically relevant profilins. Methods: The release of Phl p allergens from pollen was determined by mass spectrometry and immunochemistry. T‐cell responses, epitope mapping and cross‐reactivity to profilins (Phl p 12, Ole e 2, Bet v 2 and Mal d 4) were measured in vitro using PBMCs from 26 Spanish grass‐allergic donors IgE‐sensitized to profilin. Cross‐reactivity was addressed in vivo using 2 different mouse strains (BALB/c and C3H). Results: Phl p 12 and Phl p 1 are released from pollen simultaneously and in similar amounts. Both T‐cell response frequency (17/26 donors) and strength were comparable between Phl p 12 and Phl p 1. T‐cell cross‐reactivity to other profilins correlated with overall sequence homology, and 2 immunodominant epitope regions of Phl p 12 were identified. Data from mice immunized with Phl p 12 showed that cross‐reactivity to Bet v 2 was mediated by conserved epitopes and further influenced by additional genetic factors, likely to be MHC II. Conclusion: The strength, prevalence and cross‐reactivity of T‐cell responses towards Phl p 12 are comparable to the major allergen Phl p 1, which supports the hypothesis that T cells to Phl p 12 can play an important role in development of allergic symptoms, such as those associated with pollen‐food syndrome. [ABSTRACT FROM AUTHOR]

Abstract: Background: Little is known about the prevalence of food allergy (FA) in China. The aim of this study was to investigate the disparity of FA between urban and rural areas in southern China. Methods: EuroPrevall questionnaire responses were obtained from 5542 school‐age children in urban Guangzhou and 5319 in rural Shaoguan. A case‐control study enrolled 190 children with adverse reactions (ARs) after food intake as cases and 212 controls in Guangzhou, whereas 116 cases and 233 controls in Shaoguan. These subjects underwent skin prick test (SPT) and serum IgE measurements to food and inhalant allergens. Allergen extracts from shrimp, house dust mite (HDM), and cockroach were prepared for IgE cross‐reactivity testing in 23 Guangzhou and 20 Shaoguan shrimp‐sensitized subjects. Results: The prevalence of ARs to shrimp was higher in Guangzhou than in Shaoguan children (3.5% vs 1.4%, P < .001). However, sensitization rate to shrimp (SPT: 3.7% vs 11.2%, P = .015; IgE: 12.6% vs 36.2%, P < .001) and cockroach (SPT: 5.3% vs 33.5%; IgE: 2.6% vs 27.6%, P < .001) was lower in Guangzhou. A significant correlation between shrimp and HDM/cockroach IgE was found in Shaoguan children. The proportions of positive IgE to tropomyosin (Pen a 1, Der p 10) were lower than 7.4% in both areas. Cockroach allergen has a significantly higher inhibition rate of binding to IgE to house dust mite allergens in Shaoguan sera. Conclusion: Shrimp is a common allergic food in southern China. Higher proportion of shrimp sensitization in rural subjects could be explained by cross‐reactivity to cockroach. Tropomyosin was not a major allergen responding to the cross‐reactivity. [ABSTRACT FROM AUTHOR]

The authors report a survey carried out in a cattle farm between January and April 2009 in Mateur region (Northern Tunisia). Seroprevalence by Microscopic Agglutination Test ( MAT) was estimated to 81.4 ± 6% and 35 ± 2% in cows and calves, respectively. Seropositivity to more than one serovar was noticed in 91% (81/89) of infected animals. The examination of the distribution pattern of Leptospira serovars involved in this outbreak indicates that serovar Pomona was the predominant one (75.3%), followed by Autumnalis (59.5%), Bim (58.4%) and Munchen (55%). High titres (between 400 and 6400) were found in 68.7% of the tested animals and were correlated with clinical onset of leptospirosis. Leptospirosis is an underestimated pathogen in Tunisia; further investigations are needed to study the epidemiology both in man and animals and to implement effective control measures. [ABSTRACT FROM AUTHOR]

Background Measures to prevent occupational exposure to epoxy resins, including education, medical examination, and voluntary agreements between employers and workers, have not been effective enough to protect against skin sensitization. Therefore, alternatives to the major epoxy resin haptens that have been found to be less sensitizing in the local lymph node assay have been developed. Objectives To study the cross-reactivity of two newly designed epoxy resin monomers, with decreased skin-sensitizing potency and good technical properties as compared with diglycidyl ether of bisphenol A ( DGEBA), in subjects with known contact allergy to epoxy resin of DGEBA type. Patients and Methods Eleven individuals with previous positive patch test reactions to epoxy resin of DGEBA participated in the study. The two alternative epoxy resin monomers were synthesized and patch tested in dilution series in parallel with epoxy resin of DGEBA from the baseline series (containing 92% DGEBA). Results All participants reacted to epoxy resin of DGEBA on retesting. Three participants reacted to monomer 1. No reactions were seen to monomer 2. Conclusions The alternative monomers studied showed little or no cross-reactivity with epoxy resin of DGEBA. Decreasing the risk of sensitization by using less sensitizing compounds is important, as contact allergy to epoxy resins is common in spite of thorough preventive measures. [ABSTRACT FROM AUTHOR]

Introduction The Epstein Barr Virus (EBV) has been associated with the autoimmune disease, Systemic Lupus Erythematosus (SLE). EBV nuclear antigen-I (EBNA-1) is the major nuclear protein of EBV. We previously generated an IgG monoclonal antibody (MAb) to EBNA-1, 3D4, and demonstrated that it cross-reacts with double stranded DNA (dsDNA) and binds the 148 amino acid viral binding site (VBS) in the carboxyl region of EBNA-1. The aim of the present study was to characterize another antibody to EBNA-1 that cross-reacts with dsDNA, compare its immunoglobulin genes to 3D4, and finely map the epitope in EBNA-1 that is recognized by these cross-reactive antibodies. Methods We generated an IgM MAb to EBNA-1, 16D2, from EBNA-1 injected mice and demonstrated by ELISA that it cross-reacts with dsDNA and binds the 148 amino acid VBS. We sequenced the variable heavy and light chain genes of 3D4 and 16D2 and compared V gene usage. To more finely map the epitope in EBNA-1 recognized by these MAbs, we examined their binding by ELISA to 15 overlapping peptides spanning the 148 amino acid domain. Results Sequence analysis revealed that 3D4 and 16D2 utilize different VH and VL genes but identical JH and Jk regions with minimal junctional diversity. This accounts for similarities in their CDR3 regions and may explain their similar dual binding specificity. Epitope mapping revealed 3D4 and 16D2 bind the same peptide in the VBS. Based on the crystal structure of EBNA-1, we observed that this peptide resides at the base of an exposed proline rich loop in EBNA-1. Conclusion We have demonstrated that two MAbs that bind EBNA-1 and cross-react with dsDNA, recognize the same peptide in the VBS. This peptide may serve as a mimetope for dsDNA and may be of diagnostic and therapeutic value in SLE. [ABSTRACT FROM AUTHOR]

Background In Japan, over 2000 users of a facial soap containing Glupearl 19S ( GP19S), a hydrolysed wheat protein ( HWP), developed immediate-type systemic wheat allergy ( HWP-IWA), and ∼70% of them developed associated contact urticaria. Objectives We investigated whether HWP-IWA patients cross-react with other HWPs, and analysed HWP antigenic characteristics. Methods We used 10 types of HWP that are commercially available as cosmetic ingredients, and 16 subjects with HWP-IWA. We performed an enzyme-linked immunosorbent assay ( ELISA) to evaluate the reactivity to each HWP, and western blotting to evaluate the characteristics of the antigens by using HWP-IWA patients' serum IgE antibodies. We also performed prick tests with the HWPs. Results The patients reacted to four other HWPs in addition to GP19S, according to ELISA, and this was confirmed by strong reactions in the prick tests to the same four types of HWP. Smears of antigens with molecular weights ranging from the high range to the low range were seen on western blotting with the four HWPs that showed strong reactions in the ELISA and prick tests. Conclusions HWP-IWA patients cross-react with other HWPs. The antigens that they cross-reacted to had a molecular weight distribution similar to that of GP19S present in the HWPs. [ABSTRACT FROM AUTHOR]

Background Beside the basic resins, reactive diluents and hardeners are important sensitizers in epoxy resin systems ( ERSs). Because of chemical similarities, immunological cross-reactivity may occur. Objectives To analyse concomitant reactivity among reactive diluents and hardeners in the patients concerned, as one integral part of a research project on the sensitizing capacity of ERSs ( FP-0324). Methods A retrospective analysis of data from the Information Network of Departments of Dermatology ( IVDK), 2002-2011, was performed. Results There was close concomitant reactivity to 1,6-hexanediol diglycidyl ether and 1,4-butanediol diglycidyl ether (1,4- BDDGE), and to phenyl glycidyl ether ( PGE) and cresyl glycidyl ether ( CGE), whereas reactions to p-tert-butylphenyl glycidyl ether occurred more independently from those to PGE and CGE. Concomitant reactions to butyl glycidyl ether and 1,4- BDDGE may point to a common allergenic compound derived from the metabolism of 1,4- BDDGE. Among the structurally more diverse group of hardeners, there was no evidence of immunological cross-reactions. Conclusions More detailed knowledge of cross-reactivity among ERS components facilitates the interpretation of patch test results and will allow safer ERSs to be composed in the future. [ABSTRACT FROM AUTHOR]

The Standards of Care Committee of the British Society for Allergy and Clinical Immunology ( BSACI) and an expert panel have prepared this guidance for the management of immediate and non-immediate allergic reactions to penicillins and other beta-lactams. The guideline is intended for UK specialists in both adult and paediatric allergy and for other clinicians practising allergy in secondary and tertiary care. The recommendations are evidence based, but where evidence is lacking, the panel reached consensus. During the development of the guideline, all BSACI members were consulted using a Web-based process and all comments carefully considered. Included in the guideline are epidemiology of allergic reactions to beta-lactams, molecular structure, formulations available in the UK and a description of known beta-lactam antigenic determinants. Sections on the value and limitations of clinical history, skin testing and laboratory investigations for both penicillins and cephalosporins are included. Cross-reactivity between penicillins and cephalosporins is discussed in detail. Recommendations on oral provocation and desensitization procedures have been made. Guidance for beta-lactam allergy in children is given in a separate section. An algorithm to help the clinician in the diagnosis of patients with a history of penicillin allergy has also been included. [ABSTRACT FROM AUTHOR]

We report on the cross-reactivity of the cell adhesive peptide CRRETAWAC between human and porcine endothelial cells (ECs). CRRETAWAC is a phage display derived peptide which has been shown to bind the α5β1 receptor on human ECs, but does not bind platelets and thus could be incorporated into a coating for cardiovascular biomaterials that resists platelet adhesion and thrombosis, while allowing for endothelialization. To determine the cross-reactivity of the peptide, attachment and growth of human and porcine ECs on CRRETAWAC fluorosurfactant polymer (FSP) coated surfaces was explored. CRRETAWAC FSP was synthesized and characterized by mass spectrometry, NMR, and IR spectroscopy. pEC attachment and growth on CRRETAWAC FSP was similar to the positive controls, human fibronectin and RGD FSP, achieving confluence in 72 h. Initial adhesion on CRRETAWAC FSP was also similar for porcine and human ECs. Blocking with soluble CRRETAWAC peptide reduced adhesion to CRRETAWAC coated surfaces by over 50%, indicating that the pECs specifically bind CRRETAWAC peptide. With this study, we have demonstrated that CRRETAWAC peptide coated surfaces are capable of binding porcine ECs in a specific manner and supporting a confluent layer of pECs. In vitro validation of the porcine model was critical for ensuring the best chance of success for the in vivo testing of CRRETAWAC coated ePTFE vascular grafts. © 2013 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 102A: 2857-2863, 2014. [ABSTRACT FROM AUTHOR]

Background In 2005, methylisothiazolinone ( MI) on its own came into use as a preservative. Prior to that, MI was always present together with methylchloroisothiazolinone ( MCI). Can the pattern of reactivity to the separate active ingredients in allergic patients tell us something about the primary sensitizer? Objectives To investigate the potential pattern of cross-reactivity between the isothiazolinones tested, and to find the minimal elicitation concentration for each chemical, in order to determine whether the primary sensitizer is MCI or MI. Methods Patients reacting to MCI/ MI and/or MI were additionally patch tested with MCI/ MI, MCI, MI, 2-n-octyl-4-isothiazolin-3-one ( OIT) and 4,5-dichloro-2-n-octyl-4-isothiazolin-3-one (dichloro- OIT) in serial dilutions. Results Three different groups of reactors were seen. One group did not react to MI; another group reacted to both MCI and MI, but had higher patch test reactivity to MCI; and a third group reacted to both MCI and MI with very similar patch test reactivity, but reacted more often to OIT and dichloro- OIT. Conclusions Patch testing with the active ingredients of MCI/ MI in serial dilutions could give information on the primary sensitizer. [ABSTRACT FROM AUTHOR]

EoE patients show variable sensitization patterns to food and aeroallergens. The value of allergy testing in adult EoE patients is unclear. Component-resolved diagnosis ( CRD) may offer additional insights into sensitization patterns. The aim of this study was to characterize sensitization patterns in adult EoE patients using CRD. Serum from 76 patients (17 female), age 38.6 ± 1.5 years, was analyzed for reactivity to 112 different allergen components using an immuno-solid-phase allergen chip ( ISAC). We observed any sensitization in 59 patients (78%), of which 54 patients were polysensitized. Aeroallergen sensitization, mostly against components of grass or tree pollen, or house dust mite, was observed in 74% of the patients. Birch pollen ( rBet v 1) sensitization with cross-reactivity to food allergen components was observed in 30 patients (39%). In conclusion, food sensitizations in EoE patients are mainly caused by cross-reactivity to food allergens after primary birch pollen sensitization. Pollen and food sensitizations may cause or maintain esophageal inflammation in EoE patients. CRD provides more insight into sensitization patterns, identifies additional food allergen sensitizations and might be useful to direct dietary therapy in EoE. [ABSTRACT FROM AUTHOR]

Background Simultaneous contact allergies to Disperse Orange 1, 4-nitroaniline and p-aminodiphenylamine ( PADPA), as well as to other disperse azo dyes and to p-phenylenediamine ( PPD), have been reported. Cross-reactivity is one of the possible explanations for simultaneous reactions between PPD and disperse azo dyes. Some metabolites from the azo reduction of these disperse azo dyes could be sensitizers, as human skin bacteria produce azo reductases. Objectives To investigate the sensitizing capacity of Disperse Orange 1, PADPA and 4-nitroaniline, and the cross-reactivity between these substances and Disperse Yellow 3, its potential metabolites from azo reduction (4-aminoacetanilide and 2-amino- p-cresol), and PPD. Method The guinea-pig maximization test was used. Results It was found that both Disperse Orange 1 and PADPA are strong sensitizers and cross-react with each other. We were unable to sensitize guinea-pigs with 4-nitroaniline tested in equimolar concentrations to Disperse Orange 1. Conclusions The results indicate that patients sensitized primarily to Disperse Orange 1 will also react to PADPA, which can be found mainly in hair dyes. PPD, 4-nitroaniline, 4-aminoacetanilide, 2-amino- p-cresol and Disperse Yellow 3 did not show any cross-reactivity with Disperse Orange 1 or PADPA. [ABSTRACT FROM AUTHOR]

Background Case reports of allergy to lupin, due to primary sensitization or cross-reactions with other legumes, are increasing as a consequence of the augmented use of lupin flour in bakery, pasta formulations and other food items. The main allergens that have been associated with the sensitization to lupin are α- and β-conglutins and, to a lesser extent, γ- and δ-conglutin, but no conclusive data are available so far. The aim of this study was to characterize the sensitization pattern to lupin in a group of 12 Italian children allergic to peanut and identify the specific lupin proteins involved in the cross-reactivity with peanut. Methods The immunochemical cross-reactivity among peanut and lupin was evaluated by both in vitro immunoblotting and in vivo fresh food skin prick test ( FFSPT). Results The results showed that β-conglutin was recognized by cutaneous Ig Es from 7/12 peanut-allergic children in FFSPT and serum Ig Es from 5/12 in immunoblotting, while 4/12 and 8/12 patients tested positive to γ-conglutin in FFSPT and immunoblotting, respectively. No significant immunoreactive responses were observed to α- and δ-conglutins under non-reducing conditions, but they were bound in FFSPT by the sera of 5/12 and 3/12 patients, respectively. Conclusion In this group of allergic children, β-conglutin has been identified as the major lupin allergen involved both in vitro and in vivo cross-reactivity with peanut proteins. The role of γ-conglutin in the cross-reactivity between lupin and peanut proteins was also relevant and clear, despite the observed unspecificity of the immunoblotting responses. [ABSTRACT FROM AUTHOR]

Enzyme-linked immunosorbent assays (ELISAs) were developed for the detection of Ig G, Ig G4 and Ig E antibodies against Strongyloides stercoralis. A commercial ELISA ( IVD Research, USA) was also used, and the sensitivities and specificities of the four assays were determined. Serum samples from 26 patients with S. stercoralis infection and 55 patients with other infections or no infection were analysed. Sensitivities of the Ig G4, Ig G, Ig E and Ig G ( IVD) assays were 76·9%, 84·6%, 7·7% and 84·6%, respectively, while the specificities were 92·7%, 81·8%, 100% and 83·6%, respectively. If filariasis samples were excluded, the specificities of the Ig G4- ELISA and both Ig G- ELISAs increased to 100% and 98%, respectively. A significant positive correlation was observed between Ig G- and Ig G4- ELISAs ( r = 0·4828; P = 0·0125). Ig G- and Ig G- ( IVD) ELISAs ( r = 0·309) were positively correlated, but was not significant ( P = 0·124). Meanwhile there was no correlation between Ig G4- and Ig G- ( IVD) ELISAs ( r = 0·0042; P = 0·8294). Sera from brugian filariasis patients showed weak, positive correlation between the titres of antifilarial IgG4 and the optical densities of anti- Strongyloides Ig G4- ELISA ( r = 0·4544, P = 0·0294). In conclusion, the detection of both anti- Strongyloides Ig G4 and Ig G antibodies could improve the serodiagnosis of human strongyloidiasis. Furthermore, patients from lymphatic filariasis endemic areas who are serologically diagnosed with strongyloidiasis should also be tested for filariasis. [ABSTRACT FROM AUTHOR]

To cite this article: Aalberse RC, Crameri R. IgE-binding epitopes: a reappraisal. Allergy 2011; 66: 1261-1274. Abstract Here, we discuss various questions related to IgE epitopes: What are the technical possibilities and pitfalls, what is currently known, how can we put this information into hypothetical frameworks and the unavoidable question: how useful is this information for patient care or allergenicity prediction? We discuss the information obtained by (i) 3D structures of allergen-antibody complexes; (ii) analysis of allergen analogues; (iii) mimics without obvious structural similarity; (iv) mAbs competing with IgE; (v) repertoire analysis of cloned IgEs, and other developments. Based on limited data, four suggestions are presented in the literature: (i) IgE might be more cross-reactive than IgG; (ii) IgE might be more often directed to immunologically 'uninviting' surfaces; (iii) IgE epitopes may tend to cluster and (iv) IgE paratopes might have a higher intrinsic flexibility. While these are not proven facts, they still can generate hypotheses for future research. The hypothesis is put forward that the IgE repertoire of switched B-cells is less influenced by positive selection, because positive selection might not be able to rescue IgE-switched B cells. While this might be of interest for the discussion about mechanisms leading to allergen-sensitization, we need to be modest in answering the 'clinical relevance' question. Current evidence indicates the IgE-epitope repertoire is too big to make specific IgE epitopes a realistic target for diagnosis, treatment or allergenicity prediction. In-depth analysis of a few selected IgE epitope-peptides or mimitopes derived from allergen-sequences and from random peptide libraries, respectively, might well prove rewarding in relation to diagnosis and prognosis of allergy, particularly food allergy. [ABSTRACT FROM AUTHOR]

To cite this article: Gámez C, Sánchez-García S, Ibáñez MD, López R, Aguado E, López E, Sastre B, Sastre J, del Pozo V. Tropomyosin IgE-positive results are a good predictor of shrimp allergy. Allergy 2011; 66: 1375-1383. Abstract Background: Shrimp is a common cause of food allergy. Our aims were to determine the value of IgE antibodies in the diagnosis of shrimp allergy and to study red shrimp ( Solenocera melantho) tropomyosin both as a new allergen and as a cross-reactive IgE-binding protein. Methods: We have studied 45 subjects. Skin prick test (SPT) was carried out in all subjects, and specific IgE (sIgE) to shrimp, recombinant and natural shrimp tropomyosins rPen a 1 and nPen m 1, recombinant Der p 10, and Dermatophagoides pteronyssinus was assessed by fluoroimmunoassay and/or immunoblotting. Double-blind, placebo-controlled food challenges were carried out to confirm diagnosis of shrimp allergy. Also, in vitro inhibition tests were performed to evaluate cross-reactivity. Results: Shrimp allergy was confirmed in 18 shrimp-allergic patients. Skin prick test and IgE antibodies to shrimp were positive in all shrimp-allergic patients; sIgE to rPen a 1 was detected in 98% of these patients. Of the 18 shrimp-tolerant patients, 61% had positive SPT to shrimp, 55% were IgE-positive to shrimp, and 33% showed IgE antibodies to rPen a 1. Determination of IgE to rPen a 1 yielded a positive predictive value of 0.72 and a negative predictive value of 0.91. Conclusion: IgE levels to rPen a 1 provided additional value to the diagnosis of shrimp allergy. Some allergens in mite extract are recognized by patients who are allergic to shrimp, though their clinical relevance remains unknown. [ABSTRACT FROM AUTHOR]

Fish allergy is becoming an important health problem in Spain, a country with the third highest level of fish consumption after Japan and Portugal. The most common fish allergens are parvalbumins. In our area, the most widely consumed fish species are lean, such as whiff ( Lepidorhombus whiffiagonis) and sole ( Solea solea). Adverse reactions to fish are usually related to these species, a fact that is largely unknown to allergists in other countries. The aim of this study was to identify and purify the major allergen implicated in allergic response to sole and evaluate the IgE cross-reactivity of purified parvalbumins from whiff and sole, which are phylogenetically close, and more distant species (i.e. cod and salmon). Eighteen Spanish fish-allergic patients with a positive history of type I allergy to fish were recruited from the clinic. Total protein extracts and purified parvalbumins from whiff and sole were tested for their IgE-binding properties by combining two-dimensional Western blotting and mass spectrometry. The extent of cross-reactivity between these parvalbumins along with cod and salmon parvalbumins was investigated by IgE ELISA inhibition assay. An IgE-binding spot of approximately 14 kDa was identified as parvalbumin and confirmed as a major allergen in sole extract, which is recognized by almost 70% of the patients. Whiff parvalbumin was recognized by 83.4% of the patients. High cross-reactivity was determined for all purified parvalbumins by IgE inhibition assay. Sole and whiff parvalbumin were confirmed as major allergens. The parvalbumins of sole, whiff, cod and salmon were highly cross-reactive, thus suggesting a high amino acid sequence identity between them. Cite this as: M. Perez-Gordo, J. Cuesta- Herranz, A. S. Maroto, B. Cases, M. D. Ibáñez, F. Vivanco and C. Pastor-Vargas, Clinical & Experimental Allergy, 2011 (41) 750-758. [ABSTRACT FROM AUTHOR]

Background: Administration of imipenem-cilastatin to patients with IgE-mediated hypersensitivity to β-lactams has always been considered potentially harmful. Recent studies have demonstrated the tolerability of carbapenems (imipenem-cilastatin and meropenem) in patients with IgE-mediated hypersensitivity to β-lactams; there are no studies on this topic regarding patients with cell-mediated allergy to β-lactams. The aim of this study is to assess cross-reactivity and tolerability of imipenem in patients with cell-mediated allergy to β-lactams. Methods: From our database we selected 73 patients with cell-mediated allergy to β-lactams, diagnosed by means of immediate-type skin tests, delayed reading intradermal tests, patch tests and detection of specific IgE. Patients with negative patch tests with imipenem-cilastatin underwent an intramuscular test dosing. Results: Our patients had a total of 94 nonimmediate reactions to penicillins. All patients had positive patch tests and/or delayed reading intradermal tests for at least one of the penicillin reagent tested and negative immediate-type skin tests and specific IgE. Four patients out of 73 had a positive patch tests to at least one penicillin reagent and imipenem-cilastatin showing cross-reactivity. Sixty-four patients underwent the imipenem-cilastatin intramuscular test dosing and none of them had a clinical reaction. Conclusions: Our rate of cross-reactivity between imipenem-cilastatin and other β-lactams was 5.5%. This result is different from previous findings and this may be explained by the fact that we investigated patients with cell-mediated allergy to β-lactams. Patients with cell-mediated allergy to β-lactams should undergo patch tests and a tolerance challenge test before treatment with imipenem-cilastatin. [ABSTRACT FROM AUTHOR]

Background Reports of allergy to lupine derivatives (as de novo sensitization or cross-reactivity in subjects allergic to peanut) are increasing as their use in food products increases. Objectives The aim of this study was to assess: (1) lupine tolerance in a group of children allergic to peanut, using lupine enriched-pasta instead of raw flour as has been done in previous clinical studies; (2) whether technological treatments of lupine modify its cross-reactivity or co-sensitization with peanut; (3) the role of lupine seed proteins in sensitization, and (4) to identify the eliciting doses (EDs) by using double-blind, placebo-controlled food challenges (DBPCFC). Methods Twelve patients with a history of clinical allergic reactions to peanut were evaluated by skin prick tests (SPTs), the ImmunoCAP® test, immunoblotting, and DBPCFC. The 12 selected subjects were included in a trial where lupine-enriched pasta and placebo pasta were administered in a DBPCFC protocol. Results Positive clinical reactions were observed in two children, the EDs being 0.2 and 6.4 g of pasta, corresponding to 50 mg and 1.6 g of lupine proteins, respectively. β-conglutin was the protein most involved in SPT positivity. Conclusion Lupine-enriched pasta can be tolerated by most subjects suffering from peanut allergy, but a sizeable minority (2/12 of them in this case) can develop potentially dangerous clinical reactions. Information about possible reactions to lupine derivatives by those allergic to peanuts must be included in the labelling of lupine-enriched products to protect consumers at risk. [ABSTRACT FROM AUTHOR]

Background: Sensitization to rats and mice can develop in laboratory animal workers exposed to only one species. Reasons for this dual sensitization are unclear but may reflect a genetic predisposition to developing allergy (atopy) or alternatively cross-reactivity between rat and mouse urinary allergens. We examined cross-reactivity between rat and mouse urine and the effect atopy has on dual sensitization in laboratory animal workers. Methods: In a cross-sectional study the frequency of sensitization to rat and/or mouse was analysed in 498 employees exposed to both rat and mouse at work and 220 to rat only. RAST inhibitions, western blots and blot inhibitions were carried out on a subset of five individuals to assess cross-reactivity. Results: Fourteen per cent of workers were sensitized to rats and 9% to mouse. Over half (62%) of rat sensitized individuals were also mouse sensitized and the majority (91%) of mouse sensitized individuals were also rat sensitized. IgE cross-reactivity was demonstrated between rat and mouse urine using RAST inhibitions. Rates of atopy did not differ between rat only sensitized individuals compared with those sensitized to both species. Sensitization to cats and rabbits was more common amongst those with dual sensitization. Conclusions: Dual sensitization to rat and mouse reflects IgE cross-reactivity rather than atopy. Individuals with dual sensitization are more likely to be sensitized to other animal allergens. These findings will have implications for individuals working with only one rodent species who develop sensitization and symptoms to be aware of the potential for allergy to other species. [ABSTRACT FROM AUTHOR]

Background Specific immunotherapy is the only causal treatment of allergy available today. Traditionally, therapeutic products based on either a single grass species or a mix of such extracts are used for grass pollen immunotherapy. Investigations comparing the immunological response to these allergen preparations are needed to ensure optimal treatment. The objective of this study was to investigate patterns of T and B cell cross-reactivity to Pooideae single-species extracts and to extract mixes. Methods IgG4 induced by immunotherapy with Phleum pratense extract was investigated for cross-reactivity using nine single-species extracts and four mixes. For the mixes, studies of IgE cross-reactivity were also performed. T cell cross-reactivity was investigated in lines specific to nPhl p 1 or nPhl p 5 allergens, and the amounts of group 1 and 5 allergens in the extracts were quantified by a single radial immunodiffusion. Results The levels of treatment-induced IgG4 detected by all the extracts displayed a clear correlation to that detected by the P. pratense pollen extract. The IgE studies confirmed the cross-reactivity of P. pratense-specific B cells towards the allergens contained in the mixes, and the T cell studies demonstrated cross-reactivity towards group 1 and 5 major allergens in extracts of six temperate grass species. Conclusion Extensive T and B cell cross-reactivity was observed towards the allergens of the Pooideae grasses, and the degree of B cell cross-reactivity was independent of the number of species included in the extract mixes. This implies that treatment with pollen extract of just one Pooideae species will affect the allergic responses caused by any of the temperate grasses in this subfamily. [ABSTRACT FROM AUTHOR]

Background: Simultaneous contact allergies to the reactive diluent phenyl glycidyl ether (PGE) and epoxy resins based on diglycidyl ether of bisphenol A (DGEBA) or epoxy resins of the bisphenol F-type have been reported. The latter epoxy resins contain three isomers of diglycidyl ether of bisphenol F (DGEBF). PGE, DGEBA, and DGEBF are chemically similar with respect to the reactive glycidyl group and an aromatic ring, making cross-reactivity one of the possible explanations to simultaneous reactions. Aim: To investigate the sensitizing capacity of PGE and the cross-reactivity of PGE versus the epoxy resin monomers DGEBA and the three DGEBF monomers and vice versa. Method: The guinea-pig maximization test. Results: PGE is a strong sensitizer. Induction with DGEBA resulted in a statistically significant number of animals reacting to PGE, but when induced with PGE, the animals did not react significantly to DGEBA. Conclusions: When the results are applied to humans, it can be assumed that patients sensitized primarily to DGEBA react to PGE, but when sensitized exclusively to PGE, they do not react to DGEBA. Both reactive diluents and epoxy resins should be tested when contact allergy to epoxy resin systems are suspected. [ABSTRACT FROM AUTHOR]

Background Recently, peanut-allergic patients have reported symptoms upon ingestion of bean sprouts produced from various legumes. Objective This study was designed to identify immunoreactivity to seeds and sprouts of legumes other than peanut in sera from peanut-allergic patients. Methods Crude protein extracts of seeds and sprouts (comprising cotelydons and hypocotyls/epicotyls) of peanut, soybean, green pea, blue lupine, mung bean, alfalfa, broad bean, and azuki bean were prepared. The reactivity of sera from 10 peanut-allergic patients to these extracts was analysed by indirect histamine release (HR), enzyme-allergosorbent test (EAST), EAST inhibition, and Western blots. Skin prick tests (SPTs) were performed on the patients with fresh legume seeds as well as four commercial legume sprouts, and food challenges with soybean, pea, and lupine were performed on a subgroup of the patients. Results All legume seeds and commercial sprouts induced positive SPTs in some of the patients. Indirect HR experiments indicated an extensive co-reactivity between peanut and the legumes, and cross-reactivity was observed for soybean, pea, and lupine seeds as well as lupine hypocotyls in EAST inhibition experiments. Of the 16 protein extracts, soybean, pea, and lupine seed extracts produced visible bands in Western blots. Conclusion The symptoms reported by peanut-allergic patients after legume sprout intake might be caused by cross-reactivity of peanut-specific antibodies. The intake of raw legume sprouts might cause symptoms in peanut-allergic patients. [ABSTRACT FROM AUTHOR]

Influenza is a major cause of worldwide morbidity and mortality through frequent seasonal epidemics and infrequent pandemics. Morbidity and mortality rates from seasonal influenza are highest in the most frail, such as the elderly, those with underlying chronic conditions and very young children. Antigenic mismatch between strains recommended for vaccine formulation and circulating viruses can further reduce vaccine efficacy in these populations. Seasonal influenza vaccines with enhanced, cross-reactive immunogenicity are needed to address these problems and can confer a better immune protection, particularly in seasons were antigenic mismatch occurs. A related issue for vaccine development is the growing threat of pandemic influenza caused by H5N1 avian strains. Vaccines against strains with pandemic potential offer the best approach for reducing the potential impact of a pandemic. However, current non-adjuvanted pre-pandemic vaccines offer suboptimal immunogenicity against H5N1. For both seasonal and pre-pandemic vaccines, the addition of adjuvants may be the best approach for providing enhanced cross-reactive immunogenicity. MF59®, the first oil-in-water emulsion licensed as an adjuvant for human use, can enhance vaccine immune responses through multiple mechanisms. A trivalent MF59-adjuvanted seasonal influenza vaccine (Fluad®) has shown to induce significantly higher immune responses to influenza vaccination in the elderly, compared with non-adjuvanted vaccines, and to provide cross-reactive immunity against divergent influenza strains. Similar results have been generated with a MF59-adjuvanted H5N1 pre-pandemic vaccine, which showed higher and broader immunogenicity compared with non-adjuvanted pre-pandemic vaccines. [ABSTRACT FROM AUTHOR]

Background: Hymenoptera venom allergy can be effectively cured with specific immunotherapy, thus the correct identification of the allergen is essential. In the case of multiple skin and serum positivities it is important to know if a cross-reaction among venoms is present. We studied by CAP-inhibition assays the degree of cross-reactivity between Vespula vulgaris and Polistes dominulus. Methods: Serum samples were obtained from consecutive patients with a clinical history of grade III–IV reactions to hymenoptera sting and with nondiscriminative skin/CAP positivity to both Vespula and Polistes. Inhibition assays were carried out with a CAP method, incubating the sera separately with both venoms and subsequently measuring the specific immunoglobulin E (IgE) to venoms themselves. Results: Forty-five patients (33 male, mean age 40 years, age range 12–74, total serum IgE 242 ± 168 kU/l) were included. Their specific IgE to Vespula and Polistes were 12.03 ± 5.70 kU/l and 10.7 ± 2.0 kU/l ( P = NS), respectively. At the CAP-inhibition assays, in 25 patients a >75% heterologous inhibition by P. dominulus venom against V. vulgaris-specific IgE was found. In six subjects V. vulgaris venom effectively inhibited the P. dominulus-specific IgE. In the remaining 14 cases the CAP-inhibition test provided intermediate and not discriminative results. Conclusion: In 31/45 patients, the double sensitizations to venoms were probably the result of cross-reactions and the CAP-inhibition allowed identifying the true double sensitizations. This approach may be helpful for the correct prescription of immunotherapy in the case of V. vulgaris and P. dominulus double positivity. [ABSTRACT FROM AUTHOR]

Concomitant positive reactions to colophonium, oxidized limonene, and/or oxidized linalool are recorded in patch test studies. The main allergens in these patch test mixtures are hydroperoxides, which form antigens by a radical pathway. Theoretically, concomitant reactions can be explained not only by concomitant sensitization or by true cross-reactions but also by the hydroperoxides acting as oxidizing agents on skin proteins to form non-specific antigens without hapten–protein binding. The aim of this study was to explore concomitant reactions and cross-reactivity patterns among hydroperoxide haptens. We investigated whether individuals allergic to the main allergen in colophonium, 15-hydroperoxyabietic acid, would also react to limonene hydroperoxide or linalool hydroperoxide. Only 1 of 29 individuals reacted to more than 1 hydroperoxide. The cross-reactivity pattern among cumene hydroperoxide, limonene hydroperoxide, 1-(1-hydroperoxy-1-methylethyl) cyclohexene (cyclohexene hydroperoxide), and 15-hydroperoxydehydroabietic acid was investigated in guinea-pigs. No general cross-reactivity was observed. Cross-reactions between cumene hydroperoxide and cyclohexene hydroperoxide show that similarity in the overall structure and the way of antigen formation are needed. Quantum calculations were used to determine the formation energies of the intermediary radicals. We concluded that hydroperoxides form specific antigens and that formation of non-specific antigens is unlikely. The concomitant patch test reactions described in the literature are best explained as a result of multiple sensitizations. [ABSTRACT FROM AUTHOR]

A child allergic to cow's milk developed a mild systemic allergic reaction after the first dose of Ferplex 40® (iron proteinsuccinylate). Skin tests and in vitro studies were performed in the child, in three cow's milk-allergic controls and in a non-allergic control. Milk, casein and iron proteinsuccinylate (Ferplex 40®) were used for skin tests, specific immunoglobulin E (IgE) determination, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), immunoblotting and enzyme allergo sorbent test (EAST) inhibition. A review of the drug information sheet and contact with the manufacturer were also performed. Although proteinsuccinylate is indeed a succinylated casein (each dose containing about 575 mg of casein) there was no indication of the milk protein content in the prescribing information provided by the manufacturer. Skin tests and specific IgE were positive in the case and in all allergic controls, except for EAST to iron proteinsuccinylate in one control. In EAST, iron proteinsuccinylate in solid phase was 100% inhibited by casein and casein in solid phase was inhibited 74% by iron proteinsuccinylate. SDS-PAGE of iron proteinsuccinylate showed a broad 46 kDa band and a blur of aggregated material. On immunoblot, the patient's IgE reacted to this heavily aggregated material and in the native casein extract recognized a 35-kDa band. The allergenicity of succinylated casein (proteinsuccinylate) among milk-allergic children is demonstrated. The protein source used in drug–protein conjugates should always be indicated by the manufacturer (as it should be in foods) to avoid potential risks to allergic patients. [ABSTRACT FROM AUTHOR]