The Experts below are selected from a list of 318 Experts worldwide ranked by ideXlab platform
Jonathan Hourihane - One of the best experts on this subject based on the ideXlab platform.
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Lupin allergy in peanut allergic children and teenagers
Allergy, 2008Co-Authors: J. Shaw, G. Roberts, Kate Grimshaw, S White, Jonathan HourihaneAbstract:Background: Lupin has now been introduced into food production in the UK. There is a concern that, on account of cross-reactivity, peanut-allergic children are at high risk for Lupin allergy. AIMS: To investigate the prevalence of Lupin sensitization and allergy in children with peanut allergy compared with atopic controls. Methods: Children ( Results: Forty-seven peanut-allergic children and 46 atopic controls were recruited. Sixteen peanut-allergic children were sensitized to Lupin [34%, 95% confidence interval (CI): 21-49%]. Nine were challenged to Lupin. Two reacted (itchy mouth and urticaria; itchy mouth and 20% drop in peak expiratory flow rate) giving a minimum prevalence of Lupin allergy in peanut-allergic children of 4.0% (95% CI: 1-15%). Atopic controls were significantly (P = 0.001) less likely to be sensitized to Lupin (4%, 95% CI: 1-15%) and had smaller wheals and serum-specific IgE results. None of the atopic controls reacted on Lupin challenge, giving a rate of allergy in the atopic controls of 0% (95% CI: 0-8%). Conclusions: A small but significant number of children with peanut allergy are allergic to Lupin. Sensitization to Lupin is much rarer in nonpeanut-allergic atopic subjects.
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Lupin allergy in peanut-allergic children and teenagers.
Allergy, 2008Co-Authors: J. Shaw, G. Roberts, Kate Grimshaw, S White, Jonathan HourihaneAbstract:BACKGROUND: Lupin has now been introduced into food production in the UK. There is a concern that, on account of cross-reactivity, peanut-allergic children are at high risk for Lupin allergy.\n\nAIMS: To investigate the prevalence of Lupin sensitization and allergy in children with peanut allergy compared with atopic controls.\n\nMETHODS: Children (
Maaike M B W Dooper - One of the best experts on this subject based on the ideXlab platform.
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Characterization of IgE binding to Lupin, peanut and almond with sera from Lupin-allergic patients.
International Archives of Allergy and Immunology, 2008Co-Authors: Lise Holden, Helene Lindvik, G. B G Sletten, Christiane Kruse Fæste, Maaike M B W DooperAbstract:Background: The increasing number of applications of sweet Lupins in food is paralleled by an increase in immunoglobulin E (IgE)-mediated allergic reactions to Lupin proteins. In pa
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Characterization of IgE binding to Lupin, peanut and almond with sera from Lupin-allergic patients
International Archives of Allergy and Immunology, 2008Co-Authors: Lise Holden, Helene Lindvik, G. B G Sletten, Christiane Kruse Fæste, Maaike M B W DooperAbstract:BACKGROUND: The increasing number of applications of sweet Lupins in food is paralleled by an increase in immunoglobulin E (IgE)-mediated allergic reactions to Lupin proteins. In particular, Lupin allergy seems to appear in patients with an existing peanut allergy. In the present study, IgE-binding studies towards fractionated Lupin seed proteins, and peanut and almond proteins were performed using sera from patients with confirmed Lupin allergy. METHODS: Immunoblotting and indirect ELISA were performed to investigate IgE binding to protein extracts. ELISA inhibition experiments were performed to investigate the presence of cross-reactive allergens in the protein extracts. RESULTS: Immunoblotting and ELISA experiments demonstrated IgE binding to all Lupin conglutins (alpha, beta, gamma and delta) as well as to peanut and almond proteins, with a unique IgE-binding profile for each patient. High IgE binding to alpha-conglutin was observed and IgE from the majority of patients similarly recognized two proteins within the alpha-conglutin-containing fraction, 40 and 43 kDa in size. Inhibition ELISA experiments showed that preincubation of sera with Lupin conglutins, peanut and almond resulted in decreased IgE binding to Lupin flour. CONCLUSIONS: Overall, these results indicate that alpha-, beta-, gamma- and delta-conglutins are candidate allergens in Lupin and suggest a particularly strong allergenicity of alpha-conglutins. Furthermore, the results indicate the presence of cross-reactive allergens in Lupin, peanut and almond.
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Monoclonal antibodies against the candidate Lupin allergens alpha-conglutin and beta-conglutin.
International archives of allergy and immunology, 2007Co-Authors: Maaike M B W Dooper, Lise Holden, Christiane Kruse Fæste, Keith M Thompson, Eliann EgaasAbstract:BACKGROUND: The ingestion of dietary products containing sweet Lupin (such as Lupinus albus or Lupinus angustifolius) has been reported to cause IgE-mediated allergic reactions. Recent studies have indicated Lupin globulins as important IgE binding proteins. The aim of the present study was to generate and characterize monoclonal antibodies (mAbs) against Lupin seed proteins.\n\nMETHODS: Mice were immunized with a protein isolate from L. albus and mAbs were obtained by hybridoma techniques. Albumins and globulins were extracted, and the globulin fraction was separated further into conglutins by anion exchange chromatography. Specificities, binding patterns and applications of the mAbs were investigated by immunochemical methods.\n\nRESULTS: Five mAbs were produced: Lu11 (an IgG2b antibody), Lu8, Lu18, Lu34 and Lu35 (all IgM antibodies). The mAbs reacted strongly with protein isolates from both L. albus and L. angustifolius. All mAbs are directed towards the Lupin globulin fraction; Lu11 and Lu18 recognize alpha-conglutin, while Lu8, Lu34 and Lu35 recognize beta-conglutin. In addition, Lu11 inhibited the binding of IgE from patients with positive skin prick tests to Lupin proteins in a competitive ELISA by approximately 30%. Furthermore, preliminary results show that Lu11 can be used to develop a sensitive method for the detection of alpha-conglutin in foods.\n\nCONCLUSIONS: Lupin globulins are immunogenic and alpha-conglutin is a potential allergen. This is the first study describing mAbs against the candidate Lupin allergens, emphasizing the importance of additional studies on conglutins in Lupin allergy.
Lise Holden - One of the best experts on this subject based on the ideXlab platform.
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Characterization of IgE binding to Lupin, peanut and almond with sera from Lupin-allergic patients.
International Archives of Allergy and Immunology, 2008Co-Authors: Lise Holden, Helene Lindvik, G. B G Sletten, Christiane Kruse Fæste, Maaike M B W DooperAbstract:Background: The increasing number of applications of sweet Lupins in food is paralleled by an increase in immunoglobulin E (IgE)-mediated allergic reactions to Lupin proteins. In pa
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Lupin sensitization and clinical allergy in food allergic children in Norway.
Acta Paediatrica, 2008Co-Authors: Helene Lindvik, Lise Holden, Milada Cvancarova, Martinus Løvik, Ragnhild HalvorsenAbstract:The aim of the present pilot study was to investigate to what extent children in Norway sensitized to Lupin had clinical Lupin allergy, and to compare sensitization to Lupin with sensitization to other legumes.
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Characterization of IgE binding to Lupin, peanut and almond with sera from Lupin-allergic patients
International Archives of Allergy and Immunology, 2008Co-Authors: Lise Holden, Helene Lindvik, G. B G Sletten, Christiane Kruse Fæste, Maaike M B W DooperAbstract:BACKGROUND: The increasing number of applications of sweet Lupins in food is paralleled by an increase in immunoglobulin E (IgE)-mediated allergic reactions to Lupin proteins. In particular, Lupin allergy seems to appear in patients with an existing peanut allergy. In the present study, IgE-binding studies towards fractionated Lupin seed proteins, and peanut and almond proteins were performed using sera from patients with confirmed Lupin allergy. METHODS: Immunoblotting and indirect ELISA were performed to investigate IgE binding to protein extracts. ELISA inhibition experiments were performed to investigate the presence of cross-reactive allergens in the protein extracts. RESULTS: Immunoblotting and ELISA experiments demonstrated IgE binding to all Lupin conglutins (alpha, beta, gamma and delta) as well as to peanut and almond proteins, with a unique IgE-binding profile for each patient. High IgE binding to alpha-conglutin was observed and IgE from the majority of patients similarly recognized two proteins within the alpha-conglutin-containing fraction, 40 and 43 kDa in size. Inhibition ELISA experiments showed that preincubation of sera with Lupin conglutins, peanut and almond resulted in decreased IgE binding to Lupin flour. CONCLUSIONS: Overall, these results indicate that alpha-, beta-, gamma- and delta-conglutins are candidate allergens in Lupin and suggest a particularly strong allergenicity of alpha-conglutins. Furthermore, the results indicate the presence of cross-reactive allergens in Lupin, peanut and almond.
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Monoclonal antibodies against the candidate Lupin allergens alpha-conglutin and beta-conglutin.
International archives of allergy and immunology, 2007Co-Authors: Maaike M B W Dooper, Lise Holden, Christiane Kruse Fæste, Keith M Thompson, Eliann EgaasAbstract:BACKGROUND: The ingestion of dietary products containing sweet Lupin (such as Lupinus albus or Lupinus angustifolius) has been reported to cause IgE-mediated allergic reactions. Recent studies have indicated Lupin globulins as important IgE binding proteins. The aim of the present study was to generate and characterize monoclonal antibodies (mAbs) against Lupin seed proteins.\n\nMETHODS: Mice were immunized with a protein isolate from L. albus and mAbs were obtained by hybridoma techniques. Albumins and globulins were extracted, and the globulin fraction was separated further into conglutins by anion exchange chromatography. Specificities, binding patterns and applications of the mAbs were investigated by immunochemical methods.\n\nRESULTS: Five mAbs were produced: Lu11 (an IgG2b antibody), Lu8, Lu18, Lu34 and Lu35 (all IgM antibodies). The mAbs reacted strongly with protein isolates from both L. albus and L. angustifolius. All mAbs are directed towards the Lupin globulin fraction; Lu11 and Lu18 recognize alpha-conglutin, while Lu8, Lu34 and Lu35 recognize beta-conglutin. In addition, Lu11 inhibited the binding of IgE from patients with positive skin prick tests to Lupin proteins in a competitive ELISA by approximately 30%. Furthermore, preliminary results show that Lu11 can be used to develop a sensitive method for the detection of alpha-conglutin in foods.\n\nCONCLUSIONS: Lupin globulins are immunogenic and alpha-conglutin is a potential allergen. This is the first study describing mAbs against the candidate Lupin allergens, emphasizing the importance of additional studies on conglutins in Lupin allergy.
J. Shaw - One of the best experts on this subject based on the ideXlab platform.
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Lupin allergy in peanut allergic children and teenagers
Allergy, 2008Co-Authors: J. Shaw, G. Roberts, Kate Grimshaw, S White, Jonathan HourihaneAbstract:Background: Lupin has now been introduced into food production in the UK. There is a concern that, on account of cross-reactivity, peanut-allergic children are at high risk for Lupin allergy. AIMS: To investigate the prevalence of Lupin sensitization and allergy in children with peanut allergy compared with atopic controls. Methods: Children ( Results: Forty-seven peanut-allergic children and 46 atopic controls were recruited. Sixteen peanut-allergic children were sensitized to Lupin [34%, 95% confidence interval (CI): 21-49%]. Nine were challenged to Lupin. Two reacted (itchy mouth and urticaria; itchy mouth and 20% drop in peak expiratory flow rate) giving a minimum prevalence of Lupin allergy in peanut-allergic children of 4.0% (95% CI: 1-15%). Atopic controls were significantly (P = 0.001) less likely to be sensitized to Lupin (4%, 95% CI: 1-15%) and had smaller wheals and serum-specific IgE results. None of the atopic controls reacted on Lupin challenge, giving a rate of allergy in the atopic controls of 0% (95% CI: 0-8%). Conclusions: A small but significant number of children with peanut allergy are allergic to Lupin. Sensitization to Lupin is much rarer in nonpeanut-allergic atopic subjects.
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Lupin allergy in peanut-allergic children and teenagers.
Allergy, 2008Co-Authors: J. Shaw, G. Roberts, Kate Grimshaw, S White, Jonathan HourihaneAbstract:BACKGROUND: Lupin has now been introduced into food production in the UK. There is a concern that, on account of cross-reactivity, peanut-allergic children are at high risk for Lupin allergy.\n\nAIMS: To investigate the prevalence of Lupin sensitization and allergy in children with peanut allergy compared with atopic controls.\n\nMETHODS: Children (
Alan Robson - One of the best experts on this subject based on the ideXlab platform.
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Assessing sulfur status in Lupins and wheat
Australian Journal of Experimental Agriculture, 1995Co-Authors: Alan Robson, L. D. Osborne, K. Snowball, W.j. SimmonsAbstract:The effect of sulfur (S) supply on growth and S distribution within Lupin and wheat plants was studied in a glasshouse experiment using pots containing 11 Lupin or 15 wheat plants in 6 kg soil. Shoot growth and grain yield increased with increasing S supply, and both species produced maximum grain yield at 60 mg S/pot. Wheat yielded a lower percentage of maximum grain yield than Lupin where no S was applied. Sulfur concentrations in all shoot parts increased with increasing S supply in both wheat and Lupins. In wheat, S concentrations decreased with increasing plant age. At all rates of S, concentrations in old leaves were higher than in the youngest leaves. In Lupins, S accumulated in stems when supply was adequate but decreased markedly with S deficiency and plant age. Concentrations in other parts of Lupins generally did not change with plant age. Sulfur concentrations in the youngest open leaf blades were higher than those in old leaves at all rates of S. For Lupins, critical S concentrations in the young leaves (0.28%), stems (0.07%), and whole shoots (0.15%), and the critical nitrogen (N) to S ratio in young leaves (22), are likely to be valid as diagnostic indices for S deficiency as they do not appear to be affected by plant maturity. In contrast, critical S concentrations (0.14-0.31% S) and N to S ratio (9-19) in young leaves of wheat plants changed sharply with plant age; neither is useful as a diagnostic aid unless the maturity of the plant in known. Field surveys were conducted in the agricultural regions of Geraldton and Dowerin in Western Australia to investigate the incidence of S deficiency in Lupin and wheat crops. Sulfur concentrations in Lupins and wheat from Dowerin were higher than those sampled at Geraldton. Lupin crops from both regions and wheat from Dowerin had an adequate S supply. Of the wheat sampled at Geraldton, 36% was deficient or marginal in S.
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Seed manganese affects the early growth of Lupins in manganese-deficient conditions
Australian Journal of Agricultural Research, 1994Co-Authors: Jack Crosbie, Nancy Longnecker, Alan RobsonAbstract:Poor crop establishment and split seed associated with manganese (Mn) deficiency are major problems in the production of narrow-leafed Lupins (Lupinus angustifolius L.) in Western Australia. A survey of Western Australian seed producers indicated that Mn concentrations in Lupin seeds ranged from 8 to 62 mg kg-1, with the majority of the seed containing less than 20 mg kg-1. We studied seedling growth of Lupins (cultivars Gungurru and Danja) in nutrient solution, from seed with Mn concentrations ranging from 8 (Seed8) to 223 (Seed 223) mg kg-1. Without added Mn, the final weight of plants grown from Seed8 was 39% for shoots and 30% for roots, compared to maximum growth (Seed62). With adequate external Mn supply, there was no effect of seed Mn on growth of plants grown from undamaged seedlings. Shoot weight of Gungurru Lupins 42 days after imbibing increased with increasing seed Mn concentration up to about 55 mg kg-1 when grown without added Mn. Growth of Danja plants increased similarly with increasing seed Mn concentration.
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Variation in the growth of Lupin species and genotypes on alkaline soil
Plant and Soil, 1993Co-Authors: Caixian Caixian Tang, Nancy Longnecker, Bevan Buirchell, Alan RobsonAbstract:Commercial Lupins grow poorly on alkaline and neutral fine-textured soils. Genotypic variation exists among Lupins. The present study compared the growth of 13 Lupin genotypes, including introduced cultivars and wild types, in an alkaline loamy soil and an acid loamy soil.
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Effects of seed manganese concentration on Lupin emergence
Plant and Soil, 1993Co-Authors: Jack Crosbie, Fleur Davies, Nancy Longnecker, Alan RobsonAbstract:Seed of narrow-leafed Lupin (Lupinus angustifolius L.) produced in Western Australia often has low manganese (Mn) concentration because of low Mn availability in the soil during grain filling. A major problem of Lupin production is poor seedling establishment. We tested the hypothesis that low Mn concentration in Lupin seeds decreases emergence.
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Effects of seed manganese concentration on Lupin emergence
Plant and Soil, 1993Co-Authors: Jack Crosbie, Fleur Davies, Nancy Longnecker, Alan RobsonAbstract:Seed of narrow-leafed Lupin (Lupinus angustifolius L.) produced in Western Australia often has low manganese (Mn) concentration because of low Mn availability in the soil during grain filling. A major problem of Lupin production is poor seedling establishment. We tested the hypothesis that low Mn concentration in Lupin seeds decreases emergence. The experiment was a factorial design comparing emergence of Lupins (cv. 'Gungurru') grown under glasshouse conditions from seed with 2 different internal Mn concentrations (7 or 35 mg Mn kg-1 DW) and with 2 external Mn fertiliser treatments (0 or 10 mg MnSO4.H2O kg-1 soil). There were no visible differences between the seeds. Emergence was monitored and plants were harvested 17 days after sowing. Emergence was approximately 60% in all pots sown with low Mn compared to 100% in pots sown with high Mn seed. Application of Mn did not increase the final emergence of low Mn seed. Seed viability was assessed by staining with tetrazolium chloride, a common test used in seed testing laboratories. All high Mn seed were viable while 34% of low Mn seed were completely or partly unstained and therefore were non-viable. We have shown that low Mn supply during seed filling may lead to production of non-viable seed that cannot be visually distinguished from viable seed.. © 1993 Kluwer Academic Publishers.
