Occupational rhinitis and asthma by Lathyrus sativus flour: Characterization of allergens

Porcel, Sergio; León, Francisco; Valero, Ana; Cuevas, M.; Cuesta, E. Álvarez

doi:10.1067/mai.2001.113567

Cited by 5 publications

(3 citation statements)

References 7 publications

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“…Aside from 36 kDa, an IgE binding protein with a molecular mass of 42 kDa was also noted as a major allergen of the raw extract. Several studies on various food proteins reported that cooking may reduce allergenicity of some food allergens [28] . As observed in our study, this 42 kDa major allergen and several additional minor allergens were detected only in the raw extract.…”

Section: Discussionmentioning

confidence: 99%

Identification of the major allergen of Macrobrachium rosenbergii (giant freshwater prawn)

Yadzir

Misnan

Abdullah

et al. 2012

Asian Pacific Journal of Tropical Biomedicine

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Section: Discussionmentioning

confidence: 99%

Identification of the major allergen of Macrobrachium rosenbergii (giant freshwater prawn)

Yadzir

Misnan

Abdullah

et al. 2012

Asian Pacific Journal of Tropical Biomedicine

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“…The N-terminal amino-acid sequences of bands 1, 2 and 4 from the 80-95% ammonium sulfate fraction had homology with the 7S vicilin storage proteins of Pisum sativum and Vicia faba, while band 3 showed significant homology with other plant albumins (Fig. 1b) that are known to be associated with allergies (Porcel et al, 2001).…”

Section: Results and Disucussionmentioning

confidence: 93%

“…bronchial asthma, rhinoconjunctivitis, generalized urticaria and facial oedema) in sensitized individuals (Valdivieso et al, 1988;Ortiz et al, 2000;Porcel et al, 2001;Anton Girones et al, 2005). Allergenic proteins with molecular weights of 46, 28 and 21 kDa have been identified by IgE Western blotting in allergenic patients (Porcel et al, 2001). However, to the best of our knowledge no allergens from this plant have been fully characterized.…”

Section: Introductionmentioning

confidence: 99%

Purification, identification and preliminary crystallographic studies of an allergenic protein fromLathyrus sativus

2006

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A 24 kDa protein was purified from the seeds of Lathyrus sativus by ammonium sulfate fractionation and ion-exchange chromatography. The N-terminal aminoacid sequence showed significant homology with the 2S albumin class of seed storage proteins. The protein showed 85% sequence homology with the seed albumin of Pisum sativum within the 40 N-terminal residues. Crystals were obtained by the hanging-drop vapour-diffusion method. The crystals belonged to space group P2 1 2 1 2 1 , with unit-cell parameters a = 43.5, b = 82.7, c = 153.4 Å .

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Legume Allergens Pea, Chickpea, Lentil, Lupine and Beyond

Abu Risha,

Rick,

Plum

et al. 2024

Curr Allergy Asthma Rep

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Purpose of the Review In the last decade, an increasing trend towards a supposedly healthier vegan diet could be observed. However, recently, more cases of allergic reactions to plants and plant-based products such as meat-substitution products, which are often prepared with legumes, were reported. Here, we provide the current knowledge on legume allergen sources and the respective single allergens. We answer the question of which legumes beside the well-known food allergen sources peanut and soybean should be considered for diagnostic and therapeutic measures. Recent Findings These “non-priority” legumes, including beans, pea, lentils, chickpea, lupine, cowpea, pigeon pea, and fenugreek, are potentially new important allergen sources, causing mild-to-severe allergic reactions. Severe reactions have been described particularly for peas and lupine. An interesting aspect is the connection between anaphylactic reactions and exercise (food-dependent exercise-induced anaphylaxis), which has only recently been highlighted for legumes such as soybean, lentils and chickpea. Most allergic reactions derive from IgE cross-reactions to homologous proteins, for example between peanut and lupine, which is of particular importance for peanut-allergic individuals ignorant to these cross-reactions. Summary From our findings we conclude that there is a need for large-scale studies that are geographically distinctive because most studies are case reports, and geographic differences of allergic diseases towards these legumes have already been discovered for well-known “Big 9” allergen sources such as peanut and soybean. Furthermore, the review illustrates the need for a better molecular diagnostic for these emerging non-priority allergen sources to evaluate IgE cross-reactivities to known allergens and identify true allergic reactions.

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Occupational rhinitis and asthma by Lathyrus sativus flour: Characterization of allergens

Cited by 5 publications

References 7 publications

Identification of the major allergen of Macrobrachium rosenbergii (giant freshwater prawn)

Identification of the major allergen of Macrobrachium rosenbergii (giant freshwater prawn)

Purification, identification and preliminary crystallographic studies of an allergenic protein fromLathyrus sativus

Legume Allergens Pea, Chickpea, Lentil, Lupine and Beyond

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