A major barley allergen associated with baker's asthma disease is a glycosylated monomeric inhibitor of insect ?-amylase: cDNA cloning and chromosomal location of the gene

Mena, Montaña; Sánchez‐Monge, Rosa; Gómez, Luis; Salcedo, Gabriel; Carbonero, Pilar

doi:10.1007/bf00040604

Cited by 56 publications

(33 citation statements)

References 30 publications

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“…Both components are rye members of the BMAI-1 (a barley monomeric inhibitor which does not seem to have the corresponding wheat homologue) subfamily [6]. However, components 1 and 2 behave as homodimeric proteins and, unlike BMAI-1 [12], are not glycosylated. This last difference is likely to be responsible for the strong IgE-binding of BMAI-1 when tested with sera of allergic patients, in contrast with the lack of response of the rye components.…”

Section: Discussionmentioning

confidence: 99%

Rye Inhibitors of Animal α‐amylases Show Different Specifities, Aggregative Properties and IgE‐binding Capacities than Their Homologues from Wheat and Barley

García‐Casado

Sánchez‐Monge

López-Otı́n

et al. 1994

European Journal of Biochemistry

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Three new members of the a-amylase/trypsin-inhibitor family of cereal endosperm have been isolated from rye. N-terminal amino acid sequence comparison revealed that two of the purified proteins were the rye homologues of the barley monomeric inhibitor (BMAI-1) previously described, while the other rye protein corresponded to one of the subunits of the barley and wheat heterotetrameric inhibitors. However, the inhibitory specificities (active against human salivary a-amylase), aggregative behaviours (mainly as dimeric forms) and IgE-binding capacities (not recognized by sera from allergic patients) of the rye inhibitors were clearly different from those of their wheat and barley counterparts. These results indicate that homologous inhibitors may have distinctive properties in different cereal species.Plant proteins that inhibit a-amylases and proteinases from pests and pathogens are receiving considerable attention because of their potential role and use in plant protection [ 1, 21. A further reason to study some of these proteins (i.e. those from cereal endosperm) comes from the recent finding that they are major allergens in the allergic diseases provoked by inhalation or ingestion of cereal flours [3, 41.An inhibitor family of animal a-amylases and of trypsin, which is particularly abundant in wheat and barley endosperm, is among those that have been more actively studied (see [5, 61 for reviews). About 20 different members of this protein family, all of them with molecular masses in the 12-16-kDa range, have been characterized in these cereal species. The inhibitors of animal a-amylases can be either monomeric, homodimeric or heterotetrameric (three different subunits with one of them present in two copies), while those active against trypsin so far described are monomeric proteins. Joint consideration of the amino acid sequence similarities, the inhibitory activities and the chromosomal location of their coding genes, allows us to classify the inhibitor subunits into different subfamilies. In Triticum and Hordeum all subunits belonging to the same subfamily have similar inhibitory specificities and aggregative properties [6]. It should be mentioned that some subfamilies include components isolated from both wheat and barley, whereas others are represented by inhibitors detected in only one of these cereals [6].Knowledge of this protein family in other plant species, even within the Triticeae tribe, is still very scarce. Thus in rye, and concerning components active towards animal aamylases, although there are a few reports on their detection [7, 81, only the N-terminal amino acid sequences of two inhibitors have been reported. One of them shows a high degree of sequence similarity with a subunit of wheat and barley tetrameric inhibitors [9], but its aggregative behaviour and inhibitory activity has not been established. The second one is closely related with the subfamily of wheat homodimeric inhibitors and shows very similar properties to its Triticum counterparts [lo].We report here the characterization o...

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Section: Discussionmentioning

confidence: 99%

Rye Inhibitors of Animal α‐amylases Show Different Specifities, Aggregative Properties and IgE‐binding Capacities than Their Homologues from Wheat and Barley

García‐Casado

Sánchez‐Monge

López-Otı́n

et al. 1994

European Journal of Biochemistry

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“…In wheat and barley the glycosylated forms of WTAI-CM16, BTAICMb and BMAI-1 have been found to be the most prominent allergens, both in vi tro and in vivo (García-Casado et al, 1995;Sanchez-Monge et al, 1992). cDNA clones encoding these three proteins have also been isolated (García-Maroto et al, 1990;Medina et alA993;Mena et al, 1992). …”

Section: Allergenic Propertíesmentioning

confidence: 99%

A Multigene Family of Trypsin/α-Amylase Inhibitors from Cereals

Carbonero¹,

Garcı́a-Olmedo²

1999

Seed Proteins

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“…In this study, we focused our attention on a-amylase and trypsin inhibitors in grains, which block the key digestive hydrolases of insect guts, resulting in impaired insect growth. Since immunological and clinical data also indicate that the a-amylase/trypsin inhibitor family can lead to allergies, baker's asthma (a respiratory allergy to wheat proteins) and atopic dermatitis in humans (Mena et al 1992;Sanchezmonge et al 1992;Imaizumi et al 2000;Tatham & Shewry 2008), we also checked their specificity against human salivary and pancreatic amylases.…”

Section: Introductionmentioning

confidence: 99%

Specificity of α-amylase and trypsin inhibitor proteins in wheat against insect pests

Priya

Kumar

Kaur

et al. 2013

New Zealand Journal of Crop and Horticultural Science

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Insect pest infestation is a major cause of crop loss during storage. However, the use of chemical pesticides results in environmental pollution and may cause allergic reactions when consumed. The inhibition of insect digestive enzymes with potential proteinaceous or non-proteinaceous inhibitors could be an effective alternative approach to control infestations. In the present study, we evaluated the specificity of the inhibitor proteins a-amylase and trypsin in 54 genotypes of wheat (Triticum aestivum) against the digestive amylases of the wheat storage insects Rhyzopertha dominica and Tenebrio molitor, human salivary amylase, porcine pancreatic amylase and bovine trypsin. We found that these proteinaceous inhibitors vary in their expression between genotypes, and identified six genotypes in which inhibitor activity was high against the insects but low against human salivary and pancreatic amylase. These findings will significantly aid the selection of wheat genotypes with potential resistance against storage insects and minimum health concerns for humans.

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A major barley allergen associated with baker's asthma disease is a glycosylated monomeric inhibitor of insect ?-amylase: cDNA cloning and chromosomal location of the gene

Cited by 56 publications

References 30 publications

Rye Inhibitors of Animal α‐amylases Show Different Specifities, Aggregative Properties and IgE‐binding Capacities than Their Homologues from Wheat and Barley

Rye Inhibitors of Animal α‐amylases Show Different Specifities, Aggregative Properties and IgE‐binding Capacities than Their Homologues from Wheat and Barley

A Multigene Family of Trypsin/α-Amylase Inhibitors from Cereals

Specificity of α-amylase and trypsin inhibitor proteins in wheat against insect pests

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