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Allergenic reactivity of the melon profilin Cuc m 2 and its identification as major allergen.
Clin Exp Allergy. 2005 Aug; 35(8):1065-72.CE

Abstract

BACKGROUND

Melon allergy is commonly associated with oral allergy syndrome (OAS) and with hypersensitivity to pollens and other plant foods. No melon allergen responsible for these clinical characteristics has yet been isolated, although profilin has been proposed as a potential target.

OBJECTIVE

To isolate natural and recombinant melon profilin, to evaluate its in vivo and in vitro reactivity, and to analyse its behaviour in simulated gastric fluid (SGF) and heat treatments.

METHODS

A pool or individual sera from 23 patients, and an additional group of 10 patients, all of them with melon allergy, were analysed by in vitro and in vivo tests, respectively. Natural melon profilin (nCuc m 2) and its recombinant counterpart (rCuc m 2) were isolated by poly-l-proline affinity chromatography, and characterized by N-terminal amino acid sequencing, matrix-assisted laser desorption/ionization analysis, DNA sequencing of cDNAs encoding rCuc m 2, and immunodetection with anti-profilin antibodies. In vitro analysis included IgE immunodetection, specific IgE determination, ELISA-inhibition assays, and histamine release (HR) tests. In vivo activity of nCuc m 2 was established by skin prick testing (SPT). The effect of SGF and heat treatment on rCuc m 2 was followed by immunodetection, ELISA inhibition, and HR assays.

RESULTS

Both purified forms of melon profilin were recognized by rabbit anti-profilin antibodies and IgE of sera from allergic patients, and showed molecular sizes typical of the profilin family. nCuc m 2 had a blocked N-terminus, whereas rCuc m 2 rendered the expected N-terminal amino acid sequence, its full protein sequence being highly similar (98--71% identity) to those of profilins from plant foods and pollens. The natural allergen displayed a slightly higher IgE-binding capacity than its recombinant counterpart. Specific IgE to nCuc m 2 and rCuc m 2 was found in 100% and 78% of the 23 individual sera analysed, respectively. nCuc m 2 evoked positive SPT responses in all (10/10) patients tested, and rCuc m 2 induced HR in two out of three sera assayed. SGF treatment readily inactivated rCuc m 2, as shown by its loss of recognition by anti-profilin antibodies, lack of IgE binding, and inability to induce HR. In contrast, heat treatment did not affect the IgE-binding capacity of rCuc m 2.

CONCLUSIONS

Profilin is highly prevalent in melon-allergic patients, and promptly inactivated by SGF, as expected for an allergen mainly linked to OAS.

Authors+Show Affiliations

Unidad de Bioquímica, Departamento de Biotecnología, E.T.S. Ingenieros Agrónomos, Madrid, Spain. gabriel.salcedo@upm.esNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16120089

Citation

López-Torrejón, G, et al. "Allergenic Reactivity of the Melon Profilin Cuc M 2 and Its Identification as Major Allergen." Clinical and Experimental Allergy : Journal of the British Society for Allergy and Clinical Immunology, vol. 35, no. 8, 2005, pp. 1065-72.
López-Torrejón G, Crespo JF, Sánchez-Monge R, et al. Allergenic reactivity of the melon profilin Cuc m 2 and its identification as major allergen. Clin Exp Allergy. 2005;35(8):1065-72.
López-Torrejón, G., Crespo, J. F., Sánchez-Monge, R., Sánchez-Jiménez, M., Alvarez, J., Rodriguez, J., & Salcedo, G. (2005). Allergenic reactivity of the melon profilin Cuc m 2 and its identification as major allergen. Clinical and Experimental Allergy : Journal of the British Society for Allergy and Clinical Immunology, 35(8), 1065-72.
López-Torrejón G, et al. Allergenic Reactivity of the Melon Profilin Cuc M 2 and Its Identification as Major Allergen. Clin Exp Allergy. 2005;35(8):1065-72. PubMed PMID: 16120089.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Allergenic reactivity of the melon profilin Cuc m 2 and its identification as major allergen. AU - López-Torrejón,G, AU - Crespo,J F, AU - Sánchez-Monge,R, AU - Sánchez-Jiménez,M, AU - Alvarez,J, AU - Rodriguez,J, AU - Salcedo,G, PY - 2005/8/27/pubmed PY - 2006/1/21/medline PY - 2005/8/27/entrez SP - 1065 EP - 72 JF - Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology JO - Clin Exp Allergy VL - 35 IS - 8 N2 - BACKGROUND: Melon allergy is commonly associated with oral allergy syndrome (OAS) and with hypersensitivity to pollens and other plant foods. No melon allergen responsible for these clinical characteristics has yet been isolated, although profilin has been proposed as a potential target. OBJECTIVE: To isolate natural and recombinant melon profilin, to evaluate its in vivo and in vitro reactivity, and to analyse its behaviour in simulated gastric fluid (SGF) and heat treatments. METHODS: A pool or individual sera from 23 patients, and an additional group of 10 patients, all of them with melon allergy, were analysed by in vitro and in vivo tests, respectively. Natural melon profilin (nCuc m 2) and its recombinant counterpart (rCuc m 2) were isolated by poly-l-proline affinity chromatography, and characterized by N-terminal amino acid sequencing, matrix-assisted laser desorption/ionization analysis, DNA sequencing of cDNAs encoding rCuc m 2, and immunodetection with anti-profilin antibodies. In vitro analysis included IgE immunodetection, specific IgE determination, ELISA-inhibition assays, and histamine release (HR) tests. In vivo activity of nCuc m 2 was established by skin prick testing (SPT). The effect of SGF and heat treatment on rCuc m 2 was followed by immunodetection, ELISA inhibition, and HR assays. RESULTS: Both purified forms of melon profilin were recognized by rabbit anti-profilin antibodies and IgE of sera from allergic patients, and showed molecular sizes typical of the profilin family. nCuc m 2 had a blocked N-terminus, whereas rCuc m 2 rendered the expected N-terminal amino acid sequence, its full protein sequence being highly similar (98--71% identity) to those of profilins from plant foods and pollens. The natural allergen displayed a slightly higher IgE-binding capacity than its recombinant counterpart. Specific IgE to nCuc m 2 and rCuc m 2 was found in 100% and 78% of the 23 individual sera analysed, respectively. nCuc m 2 evoked positive SPT responses in all (10/10) patients tested, and rCuc m 2 induced HR in two out of three sera assayed. SGF treatment readily inactivated rCuc m 2, as shown by its loss of recognition by anti-profilin antibodies, lack of IgE binding, and inability to induce HR. In contrast, heat treatment did not affect the IgE-binding capacity of rCuc m 2. CONCLUSIONS: Profilin is highly prevalent in melon-allergic patients, and promptly inactivated by SGF, as expected for an allergen mainly linked to OAS. SN - 0954-7894 UR - https://www.unboundmedicine.com/medline/citation/16120089/Allergenic_reactivity_of_the_melon_profilin_Cuc_m_2_and_its_identification_as_major_allergen_ L2 - https://doi.org/10.1111/j.1365-2222.2005.02303.x DB - PRIME DP - Unbound Medicine ER -