Allergy to castor bean

Thorpe, Sara; Kemeny, David M.; Panzani, R; McGurl, Barry; Lord, M.

doi:10.1016/0091-6749(88)90053-x

Cited by 77 publications

(13 citation statements)

References 13 publications

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“…This sequence shows 80% similarity to sequences near the C terminal of English walnut and Brazil nut 2S albumins (table 3). From these data and from the high methionine content detected in the sequence analysis data of the blotted 6-kD peptide fraction, it is very likely that the 12-kD almond protein belongs to the sulphydryl-rich 2S albumin family of seed storage proteins [17, 18, 19, 20]. On the basis of the overall similarity between the 12-kD almond protein and 2S albumins (similar molecular weight and the high degree of similarity in the C-terminal amino acid sequence of 2S albumin in English walnut), the sequences from this IgE-binding almond protein were registered in the SwissProt database, under the accession number P82944, as almond 2S albumin.…”

Section: Resultsmentioning

confidence: 99%

Identification and Characterisation of the IgE-Binding Proteins 2S Albumin and Conglutin γ in Almond <i>(Prunus dulcis)</i> Seeds

Poltronieri

Cappello

Dohmae³

et al. 2002

Int Arch Allergy Immunol

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Background: Almond proteins can cause severe anaphylactic reactions in susceptible individuals. The aim of this study was the identification of IgE-binding proteins in almonds and the characterisation of these proteins by N-terminal sequencing. Methods: Five sera were selected from individuals with a positive reaction to food challenge. Sodium dodecylsulphate-polyacrylamide gel electrophoresis and immunoblotting were performed on almond seed proteins. Purified IgE-binding proteins were tested for immunoblot inhibition with sera pre-incubated with extracts of hazelnut and walnut. Results: N-terminal sequences of the 12-, 30- and 45-kD proteins were obtained. The 45- and 30-kD proteins shared the same N terminus, with 60% homology to the conglutin γ heavy chain from lupine seed (Lupinus albus) and to basic 7S globulin from soybean (Glycine max). The sequences of the N-terminal 12-kD protein and of an internal peptide obtained by endoproteinase digestion showed good homology to 2S albumin from English walnut (Jug r 1). Immunoblot inhibition experiments were performed and IgE binding to almond 2S albumin and conglutin γ was detected in the presence of cross-reacting walnut or hazelnut antigens. Conclusions: Two IgE-binding almond proteins were N-terminally sequenced and identified as almond 2S albumin and conglutin γ. Localisation and conservation of IgE binding in a 6-kD peptide obtained by endoproteinase digestion of 2S albumin was shown.

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Section: Resultsmentioning

confidence: 99%

Identification and Characterisation of the IgE-Binding Proteins 2S Albumin and Conglutin γ in Almond <i>(Prunus dulcis)</i> Seeds

Poltronieri

Cappello

Dohmae³

et al. 2002

Int Arch Allergy Immunol

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“…Depending on the protein, reduction was accompanied by a pronounced change-either a loss (10)(11)(12) or an increase (16) in the associated biochemical activity. In addition, the reduced protein showed an increase in susceptibility to proteolysis and heat (9,10,12,22). Thus, the reduction by thioredoxin brings about a structural change that dramatically alters the function as well as the life expectancy of the protein (Eq.…”

Section: [1]mentioning

confidence: 99%

Thioredoxin-linked mitigation of allergic responses to wheat

Buchanan

Adamidi

Lozano

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

132

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Thioredoxin, a ubiquitous 12-kDa regulatory disulfide protein, was found to reduce disulfide bonds of allergens (convert SOS to 2 SH) and thereby mitigate the allergenicity of commercial wheat preparations. Allergenic strength was determined by skin tests with a canine model for food allergy. Statistically significant mitigation was observed with 15 of 16 wheat-sensitive animals. The allergenicity of the protein fractions extracted from wheat f lour with the indicated solvent was also assessed: the gliadins (ethanol) were the strongest allergens, followed by glutenins (acetic acid), albumins (water), and globulins (salt water). Of the gliadins, the ␣ and ␤ fractions were most potent, followed by the ␥ and types. Thioredoxin mitigated the allergenicity associated with the major protein fractions-i.e, the gliadins (including the ␣, ␤, and ␥ types) and the glutenins-but gave less consistent results with the minor fractions, the albumins and globulins. In all cases, mitigation was specific to thioredoxin that had been reduced either enzymically by NADPH and NADPthioredoxin reductase or chemically by dithiothreitol; reduced glutathione was without significant effect. As in previous studies, thioredoxin was particularly effective in the reduction of intramolecular (intrachain) disulfide bonds. The present results demonstrate that the reduction of these disulfide bonds is accompanied by a statistically significant decrease in allergenicity of the active proteins. This decrease occurs alongside the changes identified previously-i.e., increased susceptibility to proteolysis and heat, and altered biochemical activity. The findings open the door to the testing of the thioredoxin system in the production of hypoallergenic, moredigestible foods.

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“…IgE-inhibitory CD8 T cells also can be generated by inhalation of antigen [9], but these cells express γδ TcR [10, 11]. Also, CD8 T cells that regulate IgE have been identified in studies of the IgE-potentiating effects of castor beans [12, 13, 14, 15], which is due to the sensitivity of CD8 T cells that inhibited IgE to castor bean ricin [16, 17, 18]. Depletion of CD8 T cells in vivo using an anti-rat CD8 monoclonal antibody [19]promoted IgE.…”

Section: Introductionmentioning

confidence: 99%

T Cytotoxic 1 and T Cytotoxic 2 CD8 T Cells Both Inhibit IgE Responses

Thomas

MacAry²,

Noble

et al. 2001

Int Arch Allergy Immunol

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Background: It is well recognized that CD8 T cells inhibit IgE responses. In this study, we investigated the mechanism of CD8 T cell-mediated IgE suppression by comparing the capacity of T cytotoxic 1 (Tc1) and T cytotoxic 2 (Tc2) CD8 T cells to inhibit IgE responses to ovalbumin (OVA). Methods: Tc1 and Tc2 CD8 T cells were generated from OVA^257–264-specific Vβ5.2 T cell receptor (TcR) transgenic mice by stimulation with anti-CD3 and anti-CD28 under Tc1 and Tc2 polarizing conditions. Tc1 and Tc2 Vβ5.2 TcR CD8 T cells (10⁶) were adoptively transferred to syngeneic mice, and following immunization with 100 µg of OVA/alum, serum IgE antibodies were measured by passive cutaneous anaphylaxis and expressed as the highest dilution that gave a detectable skin response. Results: Both Tc1 and Tc2 CD8 T cells from OT-I mice inhibited IgE. Conclusion: Both Tc1 and Tc2 CD8 T cells promote Th1 immunity and inhibit IgE responses. This process appears to be independent of CD8 T cell-derived IFN-γ, as both Tc2 (IFN-γ–) and Tc1 (IFN-γ+) CD8 T cells inhibited IgE.

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Allergy to castor bean

Cited by 77 publications

References 13 publications

Identification and Characterisation of the IgE-Binding Proteins 2S Albumin and Conglutin γ in Almond <i>(Prunus dulcis)</i> Seeds

Identification and Characterisation of the IgE-Binding Proteins 2S Albumin and Conglutin γ in Almond <i>(Prunus dulcis)</i> Seeds

Thioredoxin-linked mitigation of allergic responses to wheat

T Cytotoxic 1 and T Cytotoxic 2 CD8 T Cells Both Inhibit IgE Responses

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