The non-specific lipid transfer protein, Ara h 9, is an important allergen in peanut
Summary Background Plant food allergy in the Mediterranean area is mainly caused by non‐specific lipid transfer proteins (nsLTP). The aim of this study was to characterize peanut nsLTP in comparison with peach nsLTP, Pru p 3, and assess its importance in peanut allergy. Methods Peanut‐allergic patie...
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| Published in | Clinical and experimental allergy Vol. 39; no. 9; pp. 1427 - 1437 |
|---|---|
| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
Blackwell Publishing Ltd
01.09.2009
Blackwell |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0954-7894 1365-2222 1365-2222 |
| DOI | 10.1111/j.1365-2222.2009.03312.x |
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| Abstract | Summary
Background
Plant food allergy in the Mediterranean area is mainly caused by non‐specific lipid transfer proteins (nsLTP). The aim of this study was to characterize peanut nsLTP in comparison with peach nsLTP, Pru p 3, and assess its importance in peanut allergy.
Methods
Peanut‐allergic patients from Spain (n=32) were included on the basis of a positive case history and either a positive skin prick test or specific IgE to peanut. For comparison, sera of 41 peanut‐allergic subjects from outside the Mediterranean area were used. Natural Ara h 9 and two isoforms of recombinant Ara h 9, expressed in Pichia pastoris, were purified using a two‐step chromatographic procedure. Allergen characterization was carried out by N‐terminal sequencing, circular dichroism (CD) spectroscopy, immunoblotting, IgE inhibition tests and basophil histamine release assays.
Results
Compared with natural peanut nsLTP, the recombinant proteins could be purified in high amounts from yeast supernatant (45 mg/L). The identity of the proteins was verified by N‐terminal amino acid sequencing and with rabbit nsLTP‐specific antibodies. CD spectroscopy revealed similar secondary structures for all preparations and Pru p 3. The Ara h 9 isoforms showed 62–68% amino acid sequence identity with Pru p 3. IgE antibody reactivity to rAra h 9 was present in 29/32 Spanish and 6/41 non‐Mediterranean subjects. Recombinant Ara h 9 showed strong cross‐reactivity to nPru p 3 and similar IgE‐binding capacity as nAra h 9. The two Ara h 9 isoforms displayed similar IgE reactivity. In peanut‐allergic patients with concomitant peach allergy, Ara h 9 showed a weaker allergenic potency than Pru p 3 in histamine release assays.
Conclusions
Ara h 9 is a major allergen in peanut‐allergic patients from the Mediterranean area. Ara h 9 is capable of inducing histamine release from basophils, but to a lesser extent than Pru p 3. |
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| AbstractList | Plant food allergy in the Mediterranean area is mainly caused by non-specific lipid transfer proteins (nsLTP). The aim of this study was to characterize peanut nsLTP in comparison with peach nsLTP, Pru p 3, and assess its importance in peanut allergy.BACKGROUNDPlant food allergy in the Mediterranean area is mainly caused by non-specific lipid transfer proteins (nsLTP). The aim of this study was to characterize peanut nsLTP in comparison with peach nsLTP, Pru p 3, and assess its importance in peanut allergy.Peanut-allergic patients from Spain (n=32) were included on the basis of a positive case history and either a positive skin prick test or specific IgE to peanut. For comparison, sera of 41 peanut-allergic subjects from outside the Mediterranean area were used. Natural Ara h 9 and two isoforms of recombinant Ara h 9, expressed in Pichia pastoris, were purified using a two-step chromatographic procedure. Allergen characterization was carried out by N-terminal sequencing, circular dichroism (CD) spectroscopy, immunoblotting, IgE inhibition tests and basophil histamine release assays.METHODSPeanut-allergic patients from Spain (n=32) were included on the basis of a positive case history and either a positive skin prick test or specific IgE to peanut. For comparison, sera of 41 peanut-allergic subjects from outside the Mediterranean area were used. Natural Ara h 9 and two isoforms of recombinant Ara h 9, expressed in Pichia pastoris, were purified using a two-step chromatographic procedure. Allergen characterization was carried out by N-terminal sequencing, circular dichroism (CD) spectroscopy, immunoblotting, IgE inhibition tests and basophil histamine release assays.Compared with natural peanut nsLTP, the recombinant proteins could be purified in high amounts from yeast supernatant (> or =45 mg/L). The identity of the proteins was verified by N-terminal amino acid sequencing and with rabbit nsLTP-specific antibodies. CD spectroscopy revealed similar secondary structures for all preparations and Pru p 3. The Ara h 9 isoforms showed 62-68% amino acid sequence identity with Pru p 3. IgE antibody reactivity to rAra h 9 was present in 29/32 Spanish and 6/41 non-Mediterranean subjects. Recombinant Ara h 9 showed strong cross-reactivity to nPru p 3 and similar IgE-binding capacity as nAra h 9. The two Ara h 9 isoforms displayed similar IgE reactivity. In peanut-allergic patients with concomitant peach allergy, Ara h 9 showed a weaker allergenic potency than Pru p 3 in histamine release assays.RESULTSCompared with natural peanut nsLTP, the recombinant proteins could be purified in high amounts from yeast supernatant (> or =45 mg/L). The identity of the proteins was verified by N-terminal amino acid sequencing and with rabbit nsLTP-specific antibodies. CD spectroscopy revealed similar secondary structures for all preparations and Pru p 3. The Ara h 9 isoforms showed 62-68% amino acid sequence identity with Pru p 3. IgE antibody reactivity to rAra h 9 was present in 29/32 Spanish and 6/41 non-Mediterranean subjects. Recombinant Ara h 9 showed strong cross-reactivity to nPru p 3 and similar IgE-binding capacity as nAra h 9. The two Ara h 9 isoforms displayed similar IgE reactivity. In peanut-allergic patients with concomitant peach allergy, Ara h 9 showed a weaker allergenic potency than Pru p 3 in histamine release assays.Ara h 9 is a major allergen in peanut-allergic patients from the Mediterranean area. Ara h 9 is capable of inducing histamine release from basophils, but to a lesser extent than Pru p 3.CONCLUSIONSAra h 9 is a major allergen in peanut-allergic patients from the Mediterranean area. Ara h 9 is capable of inducing histamine release from basophils, but to a lesser extent than Pru p 3. SummaryBackgroundPlant food allergy in the Mediterranean area is mainly caused by non-specific lipid transfer proteins (nsLTP). The aim of this study was to characterize peanut nsLTP in comparison with peach nsLTP, Pru p 3, and assess its importance in peanut allergy.MethodsPeanut-allergic patients from Spain (n=32) were included on the basis of a positive case history and either a positive skin prick test or specific IgE to peanut. For comparison, sera of 41 peanut-allergic subjects from outside the Mediterranean area were used. Natural Ara h 9 and two isoforms of recombinant Ara h 9, expressed in Pichia pastoris, were purified using a two-step chromatographic procedure. Allergen characterization was carried out by N-terminal sequencing, circular dichroism (CD) spectroscopy, immunoblotting, IgE inhibition tests and basophil histamine release assays.ResultsCompared with natural peanut nsLTP, the recombinant proteins could be purified in high amounts from yeast supernatant ( greater than or equal to 45 mg-L). The identity of the proteins was verified by N-terminal amino acid sequencing and with rabbit nsLTP-specific antibodies. CD spectroscopy revealed similar secondary structures for all preparations and Pru p 3. The Ara h 9 isoforms showed 62-68% amino acid sequence identity with Pru p 3. IgE antibody reactivity to rAra h 9 was present in 29-32 Spanish and 6-41 non-Mediterranean subjects. Recombinant Ara h 9 showed strong cross-reactivity to nPru p 3 and similar IgE-binding capacity as nAra h 9. The two Ara h 9 isoforms displayed similar IgE reactivity. In peanut-allergic patients with concomitant peach allergy, Ara h 9 showed a weaker allergenic potency than Pru p 3 in histamine release assays.ConclusionsAra h 9 is a major allergen in peanut-allergic patients from the Mediterranean area. Ara h 9 is capable of inducing histamine release from basophils, but to a lesser extent than Pru p 3. Background Plant food allergy in the Mediterranean area is mainly caused by non‐specific lipid transfer proteins (nsLTP). The aim of this study was to characterize peanut nsLTP in comparison with peach nsLTP, Pru p 3, and assess its importance in peanut allergy. Methods Peanut‐allergic patients from Spain ( n =32) were included on the basis of a positive case history and either a positive skin prick test or specific IgE to peanut. For comparison, sera of 41 peanut‐allergic subjects from outside the Mediterranean area were used. Natural Ara h 9 and two isoforms of recombinant Ara h 9, expressed in Pichia pastoris , were purified using a two‐step chromatographic procedure. Allergen characterization was carried out by N‐terminal sequencing, circular dichroism (CD) spectroscopy, immunoblotting, IgE inhibition tests and basophil histamine release assays. Results Compared with natural peanut nsLTP, the recombinant proteins could be purified in high amounts from yeast supernatant (45 mg/L). The identity of the proteins was verified by N‐terminal amino acid sequencing and with rabbit nsLTP‐specific antibodies. CD spectroscopy revealed similar secondary structures for all preparations and Pru p 3. The Ara h 9 isoforms showed 62–68% amino acid sequence identity with Pru p 3. IgE antibody reactivity to rAra h 9 was present in 29/32 Spanish and 6/41 non‐Mediterranean subjects. Recombinant Ara h 9 showed strong cross‐reactivity to nPru p 3 and similar IgE‐binding capacity as nAra h 9. The two Ara h 9 isoforms displayed similar IgE reactivity. In peanut‐allergic patients with concomitant peach allergy, Ara h 9 showed a weaker allergenic potency than Pru p 3 in histamine release assays. Conclusions Ara h 9 is a major allergen in peanut‐allergic patients from the Mediterranean area. Ara h 9 is capable of inducing histamine release from basophils, but to a lesser extent than Pru p 3. Plant food allergy in the Mediterranean area is mainly caused by non-specific lipid transfer proteins (nsLTP). The aim of this study was to characterize peanut nsLTP in comparison with peach nsLTP, Pru p 3, and assess its importance in peanut allergy. Peanut-allergic patients from Spain (n=32) were included on the basis of a positive case history and either a positive skin prick test or specific IgE to peanut. For comparison, sera of 41 peanut-allergic subjects from outside the Mediterranean area were used. Natural Ara h 9 and two isoforms of recombinant Ara h 9, expressed in Pichia pastoris, were purified using a two-step chromatographic procedure. Allergen characterization was carried out by N-terminal sequencing, circular dichroism (CD) spectroscopy, immunoblotting, IgE inhibition tests and basophil histamine release assays. Compared with natural peanut nsLTP, the recombinant proteins could be purified in high amounts from yeast supernatant (> or =45 mg/L). The identity of the proteins was verified by N-terminal amino acid sequencing and with rabbit nsLTP-specific antibodies. CD spectroscopy revealed similar secondary structures for all preparations and Pru p 3. The Ara h 9 isoforms showed 62-68% amino acid sequence identity with Pru p 3. IgE antibody reactivity to rAra h 9 was present in 29/32 Spanish and 6/41 non-Mediterranean subjects. Recombinant Ara h 9 showed strong cross-reactivity to nPru p 3 and similar IgE-binding capacity as nAra h 9. The two Ara h 9 isoforms displayed similar IgE reactivity. In peanut-allergic patients with concomitant peach allergy, Ara h 9 showed a weaker allergenic potency than Pru p 3 in histamine release assays. Ara h 9 is a major allergen in peanut-allergic patients from the Mediterranean area. Ara h 9 is capable of inducing histamine release from basophils, but to a lesser extent than Pru p 3. Summary Background Plant food allergy in the Mediterranean area is mainly caused by non‐specific lipid transfer proteins (nsLTP). The aim of this study was to characterize peanut nsLTP in comparison with peach nsLTP, Pru p 3, and assess its importance in peanut allergy. Methods Peanut‐allergic patients from Spain (n=32) were included on the basis of a positive case history and either a positive skin prick test or specific IgE to peanut. For comparison, sera of 41 peanut‐allergic subjects from outside the Mediterranean area were used. Natural Ara h 9 and two isoforms of recombinant Ara h 9, expressed in Pichia pastoris, were purified using a two‐step chromatographic procedure. Allergen characterization was carried out by N‐terminal sequencing, circular dichroism (CD) spectroscopy, immunoblotting, IgE inhibition tests and basophil histamine release assays. Results Compared with natural peanut nsLTP, the recombinant proteins could be purified in high amounts from yeast supernatant (45 mg/L). The identity of the proteins was verified by N‐terminal amino acid sequencing and with rabbit nsLTP‐specific antibodies. CD spectroscopy revealed similar secondary structures for all preparations and Pru p 3. The Ara h 9 isoforms showed 62–68% amino acid sequence identity with Pru p 3. IgE antibody reactivity to rAra h 9 was present in 29/32 Spanish and 6/41 non‐Mediterranean subjects. Recombinant Ara h 9 showed strong cross‐reactivity to nPru p 3 and similar IgE‐binding capacity as nAra h 9. The two Ara h 9 isoforms displayed similar IgE reactivity. In peanut‐allergic patients with concomitant peach allergy, Ara h 9 showed a weaker allergenic potency than Pru p 3 in histamine release assays. Conclusions Ara h 9 is a major allergen in peanut‐allergic patients from the Mediterranean area. Ara h 9 is capable of inducing histamine release from basophils, but to a lesser extent than Pru p 3. |
| Author | Pokoj, S. Dueringer, N. Vieths, S. Rehm, S. Zoccatelli, G. Miguel-Moncin, M. S. Cistero-Bahima, A. Scheurer, S. Lauer, I. Reese, G. Lidholm, J. Enrique, E. |
| Author_xml | – sequence: 1 givenname: I. surname: Lauer fullname: Lauer, I. organization: Division of Allergology, Paul-Ehrlich-Institut, Langen, Germany – sequence: 2 givenname: N. surname: Dueringer fullname: Dueringer, N. organization: Division of Allergology, Paul-Ehrlich-Institut, Langen, Germany – sequence: 3 givenname: S. surname: Pokoj fullname: Pokoj, S. organization: Division of Allergology, Paul-Ehrlich-Institut, Langen, Germany – sequence: 4 givenname: S. surname: Rehm fullname: Rehm, S. organization: Division of Allergology, Paul-Ehrlich-Institut, Langen, Germany – sequence: 5 givenname: G. surname: Zoccatelli fullname: Zoccatelli, G. organization: Laboratory of Food Technology, Department of Biotechnologies, University of Verona, Verona, Italy – sequence: 6 givenname: G. surname: Reese fullname: Reese, G. organization: Division of Allergology, Paul-Ehrlich-Institut, Langen, Germany – sequence: 7 givenname: M. S. surname: Miguel-Moncin fullname: Miguel-Moncin, M. S. organization: Allergy Department Pius Hospital de Valls, Xarxa Santa Tecla, Tarragona, Spain – sequence: 8 givenname: A. surname: Cistero-Bahima fullname: Cistero-Bahima, A. organization: Allergy Department, Institut Universitari Dexeus, Barcelona, Spain – sequence: 9 givenname: E. surname: Enrique fullname: Enrique, E. organization: Hospital General de Castellon, Allergy Division, Castellon, Spain and – sequence: 10 givenname: J. surname: Lidholm fullname: Lidholm, J. organization: Phadia AB, Uppsala, Sweden – sequence: 11 givenname: S. surname: Vieths fullname: Vieths, S. organization: Division of Allergology, Paul-Ehrlich-Institut, Langen, Germany – sequence: 12 givenname: S. surname: Scheurer fullname: Scheurer, S. organization: Division of Allergology, Paul-Ehrlich-Institut, Langen, Germany |
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| Keywords | Immunopathology Food allergy Peanut Immunology Ara h 9 Lipid transfer protein peanut allergen Digestive diseases Pru p 3 Groundnut Allergen |
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| PublicationTitle | Clinical and experimental allergy |
| PublicationTitleAlternate | Clin Exp Allergy |
| PublicationYear | 2009 |
| Publisher | Blackwell Publishing Ltd Blackwell |
| Publisher_xml | – name: Blackwell Publishing Ltd – name: Blackwell |
| References | Zuidmeer L, Salentijn E, Rivas MF et al. The role of profilin and lipid transfer protein in strawberry allergy in the Mediterranean area. Clin Exp Allergy 2006; 36:666-75. Pastorello EA, Farioli L, Pravettoni V et al. The major allergen of peach (Prunus persica) is a lipid transfer protein. J Allergy Clin Immunol 1999; 103:520-6. Schocker F, Luttkopf D, Scheurer S et al. Recombinant lipid transfer protein Cor a 8 from hazelnut: a new tool for in vitro diagnosis of potentially severe hazelnut allergy. J Allergy Clin Immunol 2004; 113:141-7. Grundy J, Matthews S, Bateman B, Dean T, Arshad SH. Rising prevalence of allergy to peanut in children: data from 2 sequential cohorts. J Allergy Clin Immunol 2002; 110:784-9. Osterballe M, Hansen TK, Mortz CG, Host A, Bindslev-Jensen C. The prevalence of food hypersensitivity in an unselected population of children and adults. Pediatr Allergy Immunol 2005; 16:567-73. Lauer I, Alessandri S, Pokoj S et al. Expression and characterization of three important panallergens from hazelnut. Mol Nutr Food Res 2008; 52(Suppl. 2):S262-71. King TP. IUIS allergen nomenclature subcommittee. Bull WHO 1994; 72:796-806. Koppelman SJ, De Jong GA, Laaper-Ertmann M et al. Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2. Clin Exp Allergy 2005; 35:490-7. Kleine BI, De Heer PG, Van Der Zee JS, Aalberse RC. The stripped basophil histamine release bioassay as a tool for the detection of allergen-specific IgE in serum. Int Arch Allergy Immunol 2001; 126:277-85. Tariq SM, Stevens M, Matthews S, Ridout S, Twiselton R, Hide DW. Cohort study of peanut and tree nut sensitisation by age of 4 years. BMJ 1996; 313:514-7. Pasquato N, Berni R, Folli C et al. Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens. J Mol Biol 2006; 356:684-94. Morisset M, Moneret-Vautrin DA, Kanny G. Prevalence of peanut sensitization in a population of 4,737 subjects - an Allergo-Vigilance Network enquiry carried out in 2002. Eur Ann Allergy Clin Immunol 2005; 37:54-7. Pons L, Chery C, Mrabet N, Schohn H, Lapicque F, Gueant JL. Purification and cloning of two high molecular mass isoforms of peanut seed oleosin encoded by cDNAs of equal sizes. Plant Physiol Biochem 2005; 43:659-68. Foetisch K, Westphal S, Lauer I et al. Biological activity of IgE specific for cross-reactive carbohydrate determinants. J Allergy Clin Immunol 2003; 111:889-96. Pastorello EA, Pravettoni V, Farioli L et al. Clinical role of a lipid transfer protein that acts as a new apple-specific allergen. J Allergy Clin Immunol 1999; 104:1099-106. Sancho AI, Rigby NM, Zuidmeer L et al. The effect of thermal processing on the IgE reactivity of the non-specific lipid transfer protein from apple, Mal d 3. Allergy 2005; 60:1262-8. Daly R, Hearn MT. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J Mol Recognit 2005; 18:119-38. Ferreira F, Briza P, Infuhr D et al. Modified recombinant allergens for safer immunotherapy. Inflamm Allergy Drug Targets 2006; 5:5-14. Dreborg S, Frew A. Position paper: allergen standardization and skin tests. The European Academy of Allergology and Clinical Immunology. Allergy 1993; 48:48-82. Diaz-Perales A, Garcia-Casado G, Sanchez-Monge R, Garcia-Selles FJ, Barber D, Salcedo G. cDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family. Clin Exp Allergy 2002; 32:87-92. Fernandez-Rivas M, Gonzalez-Mancebo E, Rodriguez-Perez R et al. Clinically relevant peach allergy is related to peach lipid transfer protein, Pru p 3, in the Spanish population. J Allergy Clin Immunol 2003; 112:789-95. Marknell DA, Niederberger V, Lehtonen P et al. Molecular and immunological characterization of a novel timothy grass (Phleum pratense) pollen allergen, Phl p 11. Clin Exp Allergy 2002; 32:1329-40. Sicherer SH, Sampson HA. Peanut allergy: emerging concepts and approaches for an apparent epidemic. J Allergy Clin Immunol 2007; 120:491-503. Kleber-Janke T, Crameri R, Scheurer S, Vieths S, Becker WM. Patient-tailored cloning of allergens by phage display: peanut (Arachis hypogaea) profilin, a food allergen derived from a rare mRNA. J Chromatogr B Biomed Sci Appl 2001; 756:295-305. De Leon MP, Rolland JM, O'Hehir RE. The peanut allergy epidemic: allergen molecular characterisation and prospects for specific therapy. Expert Rev Mol Med 2007; 9:1-18. Koppelman SJ, Knol EF, Vlooswijk RA et al. Peanut allergen Ara h 3: isolation from peanuts and biochemical characterization. Allergy 2003; 58:1144-51. Schmidt M, Hoffman DR. Expression systems for production of recombinant allergens. Int Arch Allergy Immunol 2002; 128:264-70. Sicherer SH, Munoz-Furlong A, Sampson HA. Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey: a 5-year follow-up study. J Allergy Clin Immunol 2003; 112:1203-7. Lauer I, Miguel-Moncin MS, Abel T et al. Identification of a plane pollen lipid transfer protein (Pla a 3) and its immunological relation to the peach lipid-transfer protein, Pru p 3. Clin Exp Allergy 2007; 37:261-9. Lidholm J, Ballmer-Weber BK, Mari A, Vieths S. Component-resolved diagnostics in food allergy. Curr Opin Allergy Clin Immunol 2006; 6:234-40. Pons L, Chery C, Romano A, Namour F, Artesani MC, Gueant JL. The 18 kDa peanut oleosin is a candidate allergen for IgE-mediated reactions to peanuts. Allergy 2002; 57 (Suppl. 72):88-93. Davie JR. Two-dimensional gel systems for rapid histone analysis for use in minislab polyacrylamide gel electrophoresis. Anal Biochem 1982; 120:276-81. Mittag D, Akkerdaas J, Ballmer-Weber BK et al. Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J Allergy Clin Immunol 2004; 114:1410-7. Asero R, Mistrello G, Roncarolo D et al. Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion. Int Arch Allergy Immunol 2001; 124:67-9. Segura A, Moreno M, Garcia-Olmedo F. Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinach. FEBS Lett 1993; 332:243-6. Scheurer S, Pastorello EA, Wangorsch A, Kastner M, Haustein D, Vieths S. Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy. J Allergy Clin Immunol 2001; 107:724-31. Scheurer S, Lauer I, Foetisch K et al. Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion. J Allergy Clin Immunol 2004; 114:900-7. Mothes N, Valenta R, Spitzauer S. Allergy testing: the role of recombinant allergens. Clin Chem Lab Med 2006; 44:125-32. Schimek EM, Zwolfer B, Briza P et al. Gastrointestinal digestion of Bet v 1-homologous food allergens destroys their mediator-releasing, but not T cell-activating, capacity. J Allergy Clin Immunol 2005; 116:1327-33. Enrique E, Utz M, De Mateo JA, Castello JV, Malek T, Pineda F. Allergy to lipid transfer proteins: cross-reactivity among pome-granate, hazelnut, and peanut. Ann Allergy Asthma Immunol 2006; 96:122-3. 1993; 48 2001; 124 2006; 96 2002; 110 2002; 57 2005; 116 2002; 32 2006; 36 2007; 120 2003; 58 2006; 5 1982; 120 2005; 43 2006; 6 1999; 103 2005; 60 2008; 52 2001; 107 1999; 104 2003; 112 2001; 126 2003; 111 2006; 356 2007; 37 2004; 114 2004; 113 2006; 44 2002; 128 2007; 9 1996; 313 2005; 37 2005; 16 2001; 756 1994; 72 2005; 18 2005; 35 1993; 332 Daly R (e_1_2_6_38_2) 2005; 18 Grundy J (e_1_2_6_5_2) 2002; 110 Morisset M (e_1_2_6_6_2) 2005; 37 De Leon MP (e_1_2_6_8_2) 2007; 9 e_1_2_6_31_2 e_1_2_6_30_2 Asero R (e_1_2_6_23_2) 2001; 124 e_1_2_6_18_2 e_1_2_6_19_2 Sicherer SH (e_1_2_6_2_2) 2007; 120 Enrique E (e_1_2_6_15_2) 2006; 96 e_1_2_6_12_2 e_1_2_6_35_2 e_1_2_6_13_2 e_1_2_6_34_2 e_1_2_6_16_2 Lauer I (e_1_2_6_26_2) 2008; 52 e_1_2_6_39_2 e_1_2_6_17_2 e_1_2_6_14_2 e_1_2_6_37_2 e_1_2_6_36_2 Kleber‐Janke T (e_1_2_6_11_2) 2001; 756 e_1_2_6_41_2 e_1_2_6_40_2 Koppelman SJ (e_1_2_6_9_2) 2003; 58 Schocker F (e_1_2_6_20_2) 2004; 113 King TP. (e_1_2_6_32_2) 1994; 72 Mothes N (e_1_2_6_33_2) 2006; 44 e_1_2_6_7_2 e_1_2_6_29_2 e_1_2_6_3_2 Sicherer SH (e_1_2_6_4_2) 2003; 112 Dreborg S (e_1_2_6_28_2) 1993; 48 Koppelman SJ (e_1_2_6_10_2) 2005; 35 e_1_2_6_24_2 e_1_2_6_22_2 e_1_2_6_21_2 e_1_2_6_27_2 e_1_2_6_25_2 |
| References_xml | – reference: Kleber-Janke T, Crameri R, Scheurer S, Vieths S, Becker WM. Patient-tailored cloning of allergens by phage display: peanut (Arachis hypogaea) profilin, a food allergen derived from a rare mRNA. J Chromatogr B Biomed Sci Appl 2001; 756:295-305. – reference: Pasquato N, Berni R, Folli C et al. Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens. J Mol Biol 2006; 356:684-94. – reference: Marknell DA, Niederberger V, Lehtonen P et al. Molecular and immunological characterization of a novel timothy grass (Phleum pratense) pollen allergen, Phl p 11. Clin Exp Allergy 2002; 32:1329-40. – reference: Mothes N, Valenta R, Spitzauer S. Allergy testing: the role of recombinant allergens. Clin Chem Lab Med 2006; 44:125-32. – reference: Tariq SM, Stevens M, Matthews S, Ridout S, Twiselton R, Hide DW. Cohort study of peanut and tree nut sensitisation by age of 4 years. BMJ 1996; 313:514-7. – reference: Koppelman SJ, Knol EF, Vlooswijk RA et al. Peanut allergen Ara h 3: isolation from peanuts and biochemical characterization. Allergy 2003; 58:1144-51. – reference: Grundy J, Matthews S, Bateman B, Dean T, Arshad SH. Rising prevalence of allergy to peanut in children: data from 2 sequential cohorts. J Allergy Clin Immunol 2002; 110:784-9. – reference: Enrique E, Utz M, De Mateo JA, Castello JV, Malek T, Pineda F. Allergy to lipid transfer proteins: cross-reactivity among pome-granate, hazelnut, and peanut. Ann Allergy Asthma Immunol 2006; 96:122-3. – reference: Schocker F, Luttkopf D, Scheurer S et al. Recombinant lipid transfer protein Cor a 8 from hazelnut: a new tool for in vitro diagnosis of potentially severe hazelnut allergy. J Allergy Clin Immunol 2004; 113:141-7. – reference: Morisset M, Moneret-Vautrin DA, Kanny G. Prevalence of peanut sensitization in a population of 4,737 subjects - an Allergo-Vigilance Network enquiry carried out in 2002. Eur Ann Allergy Clin Immunol 2005; 37:54-7. – reference: Pastorello EA, Farioli L, Pravettoni V et al. The major allergen of peach (Prunus persica) is a lipid transfer protein. J Allergy Clin Immunol 1999; 103:520-6. – reference: Daly R, Hearn MT. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J Mol Recognit 2005; 18:119-38. – reference: Segura A, Moreno M, Garcia-Olmedo F. Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinach. FEBS Lett 1993; 332:243-6. – reference: Foetisch K, Westphal S, Lauer I et al. Biological activity of IgE specific for cross-reactive carbohydrate determinants. J Allergy Clin Immunol 2003; 111:889-96. – reference: Pons L, Chery C, Mrabet N, Schohn H, Lapicque F, Gueant JL. Purification and cloning of two high molecular mass isoforms of peanut seed oleosin encoded by cDNAs of equal sizes. Plant Physiol Biochem 2005; 43:659-68. – reference: Schimek EM, Zwolfer B, Briza P et al. Gastrointestinal digestion of Bet v 1-homologous food allergens destroys their mediator-releasing, but not T cell-activating, capacity. J Allergy Clin Immunol 2005; 116:1327-33. – reference: Lauer I, Alessandri S, Pokoj S et al. Expression and characterization of three important panallergens from hazelnut. Mol Nutr Food Res 2008; 52(Suppl. 2):S262-71. – reference: Dreborg S, Frew A. Position paper: allergen standardization and skin tests. The European Academy of Allergology and Clinical Immunology. Allergy 1993; 48:48-82. – reference: Lauer I, Miguel-Moncin MS, Abel T et al. Identification of a plane pollen lipid transfer protein (Pla a 3) and its immunological relation to the peach lipid-transfer protein, Pru p 3. Clin Exp Allergy 2007; 37:261-9. – reference: Schmidt M, Hoffman DR. Expression systems for production of recombinant allergens. Int Arch Allergy Immunol 2002; 128:264-70. – reference: Zuidmeer L, Salentijn E, Rivas MF et al. The role of profilin and lipid transfer protein in strawberry allergy in the Mediterranean area. Clin Exp Allergy 2006; 36:666-75. – reference: Sicherer SH, Sampson HA. Peanut allergy: emerging concepts and approaches for an apparent epidemic. J Allergy Clin Immunol 2007; 120:491-503. – reference: Scheurer S, Lauer I, Foetisch K et al. Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion. J Allergy Clin Immunol 2004; 114:900-7. – reference: Kleine BI, De Heer PG, Van Der Zee JS, Aalberse RC. The stripped basophil histamine release bioassay as a tool for the detection of allergen-specific IgE in serum. Int Arch Allergy Immunol 2001; 126:277-85. – reference: Sancho AI, Rigby NM, Zuidmeer L et al. The effect of thermal processing on the IgE reactivity of the non-specific lipid transfer protein from apple, Mal d 3. Allergy 2005; 60:1262-8. – reference: Diaz-Perales A, Garcia-Casado G, Sanchez-Monge R, Garcia-Selles FJ, Barber D, Salcedo G. cDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family. Clin Exp Allergy 2002; 32:87-92. – reference: Davie JR. Two-dimensional gel systems for rapid histone analysis for use in minislab polyacrylamide gel electrophoresis. Anal Biochem 1982; 120:276-81. – reference: Pastorello EA, Pravettoni V, Farioli L et al. Clinical role of a lipid transfer protein that acts as a new apple-specific allergen. J Allergy Clin Immunol 1999; 104:1099-106. – reference: Osterballe M, Hansen TK, Mortz CG, Host A, Bindslev-Jensen C. The prevalence of food hypersensitivity in an unselected population of children and adults. Pediatr Allergy Immunol 2005; 16:567-73. – reference: Mittag D, Akkerdaas J, Ballmer-Weber BK et al. Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J Allergy Clin Immunol 2004; 114:1410-7. – reference: Koppelman SJ, De Jong GA, Laaper-Ertmann M et al. Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2. Clin Exp Allergy 2005; 35:490-7. – reference: Lidholm J, Ballmer-Weber BK, Mari A, Vieths S. Component-resolved diagnostics in food allergy. Curr Opin Allergy Clin Immunol 2006; 6:234-40. – reference: Scheurer S, Pastorello EA, Wangorsch A, Kastner M, Haustein D, Vieths S. Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy. J Allergy Clin Immunol 2001; 107:724-31. – reference: Ferreira F, Briza P, Infuhr D et al. Modified recombinant allergens for safer immunotherapy. Inflamm Allergy Drug Targets 2006; 5:5-14. – reference: Asero R, Mistrello G, Roncarolo D et al. Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion. Int Arch Allergy Immunol 2001; 124:67-9. – reference: Pons L, Chery C, Romano A, Namour F, Artesani MC, Gueant JL. The 18 kDa peanut oleosin is a candidate allergen for IgE-mediated reactions to peanuts. Allergy 2002; 57 (Suppl. 72):88-93. – reference: Sicherer SH, Munoz-Furlong A, Sampson HA. Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey: a 5-year follow-up study. J Allergy Clin Immunol 2003; 112:1203-7. – reference: De Leon MP, Rolland JM, O'Hehir RE. The peanut allergy epidemic: allergen molecular characterisation and prospects for specific therapy. Expert Rev Mol Med 2007; 9:1-18. – reference: Fernandez-Rivas M, Gonzalez-Mancebo E, Rodriguez-Perez R et al. Clinically relevant peach allergy is related to peach lipid transfer protein, Pru p 3, in the Spanish population. J Allergy Clin Immunol 2003; 112:789-95. – reference: King TP. IUIS allergen nomenclature subcommittee. Bull WHO 1994; 72:796-806. – volume: 124 start-page: 67 year: 2001 end-page: 9 article-title: Lipid transfer protein publication-title: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion – volume: 36 start-page: 666 year: 2006 end-page: 75 article-title: The role of profilin and lipid transfer protein in strawberry allergy in the Mediterranean area publication-title: Clin Exp Allergy – volume: 48 start-page: 48 year: 1993 end-page: 82 article-title: Position paper publication-title: allergen standardization and skin tests. The European Academy of Allergology and Clinical Immunology – volume: 18 start-page: 119 year: 2005 end-page: 38 article-title: Expression of heterologous proteins in publication-title: a useful experimental tool in protein engineering and production – volume: 16 start-page: 567 year: 2005 end-page: 73 article-title: The prevalence of food hypersensitivity in an unselected population of children and adults publication-title: Pediatr Allergy Immunol – volume: 35 start-page: 490 year: 2005 end-page: 7 article-title: Purification and immunoglobulin E‐binding properties of peanut allergen Ara h 6 publication-title: evidence for cross-reactivity with Ara h 2 – volume: 58 start-page: 1144 year: 2003 end-page: 51 article-title: Peanut allergen Ara h 3 publication-title: isolation from peanuts and biochemical characterization – volume: 756 start-page: 295 year: 2001 end-page: 305 article-title: Patient‐tailored cloning of allergens by phage display publication-title: peanut (Arachis hypogaea) profilin, a food allergen derived from a rare mRNA – volume: 332 start-page: 243 year: 1993 end-page: 6 article-title: Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinach publication-title: FEBS Lett – volume: 6 start-page: 234 year: 2006 end-page: 40 article-title: Component‐resolved diagnostics in food allergy publication-title: Curr Opin Allergy Clin Immunol – volume: 128 start-page: 264 year: 2002 end-page: 70 article-title: Expression systems for production of recombinant allergens publication-title: Int Arch Allergy Immunol – volume: 116 start-page: 1327 year: 2005 end-page: 33 article-title: Gastrointestinal digestion of Bet v 1‐homologous food allergens destroys their mediator‐releasing, but not T cell‐activating, capacity publication-title: J Allergy Clin Immunol – volume: 103 start-page: 520 year: 1999 end-page: 6 article-title: The major allergen of peach ( ) is a lipid transfer protein publication-title: J Allergy Clin Immunol – volume: 104 start-page: 1099 year: 1999 end-page: 106 article-title: Clinical role of a lipid transfer protein that acts as a new apple‐specific allergen publication-title: J Allergy Clin Immunol – volume: 37 start-page: 261 year: 2007 end-page: 9 article-title: Identification of a plane pollen lipid transfer protein (Pla a 3) and its immunological relation to the peach lipid‐transfer protein, Pru p 3 publication-title: Clin Exp Allergy – volume: 120 start-page: 491 year: 2007 end-page: 503 article-title: Peanut allergy publication-title: emerging concepts and approaches for an apparent epidemic – volume: 32 start-page: 1329 year: 2002 end-page: 40 article-title: Molecular and immunological characterization of a novel timothy grass ( ) pollen allergen, Phl p 11 publication-title: Clin Exp Allergy – volume: 5 start-page: 5 year: 2006 end-page: 14 article-title: Modified recombinant allergens for safer immunotherapy publication-title: Inflamm Allergy Drug Targets – volume: 32 start-page: 87 year: 2002 end-page: 92 article-title: cDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid‐transfer protein family publication-title: Clin Exp Allergy – volume: 9 start-page: 1 year: 2007 end-page: 18 article-title: The peanut allergy epidemic publication-title: allergen molecular characterisation and prospects for specific therapy – volume: 107 start-page: 724 year: 2001 end-page: 31 article-title: Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy publication-title: J Allergy Clin Immunol – volume: 356 start-page: 684 year: 2006 end-page: 94 article-title: Crystal structure of peach Pru p 3, the prototypic member of the family of plant non‐specific lipid transfer protein pan‐allergens publication-title: J Mol Biol – volume: 96 start-page: 122 year: 2006 end-page: 3 article-title: Allergy to lipid transfer proteins publication-title: cross-reactivity among pome-granate, hazelnut, and peanut – volume: 120 start-page: 276 year: 1982 end-page: 81 article-title: Two‐dimensional gel systems for rapid histone analysis for use in minislab polyacrylamide gel electrophoresis publication-title: Anal Biochem – volume: 57 start-page: 88 issue: (Suppl. 72) year: 2002 end-page: 93 article-title: The 18 kDa peanut oleosin is a candidate allergen for IgE‐mediated reactions to peanuts publication-title: Allergy – volume: 112 start-page: 789 year: 2003 end-page: 95 article-title: Clinically relevant peach allergy is related to peach lipid transfer protein, Pru p 3, in the Spanish population publication-title: J Allergy Clin Immunol – volume: 114 start-page: 1410 year: 2004 end-page: 7 article-title: Ara h 8, a Bet v 1‐homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy publication-title: J Allergy Clin Immunol – volume: 37 start-page: 54 year: 2005 end-page: 7 article-title: Prevalence of peanut sensitization in a population of 4,737 subjects – an Allergo‐Vigilance Network enquiry carried out in 2002 publication-title: Eur Ann Allergy Clin Immunol – volume: 110 start-page: 784 year: 2002 end-page: 9 article-title: Rising prevalence of allergy to peanut in children publication-title: data from 2 sequential cohorts – volume: 52 start-page: S262 issue: Suppl. 2 year: 2008 end-page: 71 article-title: Expression and characterization of three important panallergens from hazelnut publication-title: Mol Nutr Food Res – volume: 43 start-page: 659 year: 2005 end-page: 68 article-title: Purification and cloning of two high molecular mass isoforms of peanut seed oleosin encoded by cDNAs of equal sizes publication-title: Plant Physiol Biochem – volume: 114 start-page: 900 year: 2004 end-page: 7 article-title: Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion publication-title: J Allergy Clin Immunol – volume: 60 start-page: 1262 year: 2005 end-page: 8 article-title: The effect of thermal processing on the IgE reactivity of the non‐specific lipid transfer protein from apple, Mal d 3 publication-title: Allergy – volume: 126 start-page: 277 year: 2001 end-page: 85 article-title: The stripped basophil histamine release bioassay as a tool for the detection of allergen‐specific IgE in serum publication-title: Int Arch Allergy Immunol – volume: 72 start-page: 796 year: 1994 end-page: 806 article-title: IUIS allergen nomenclature subcommittee publication-title: Bull WHO – volume: 44 start-page: 125 year: 2006 end-page: 32 article-title: Allergy testing publication-title: the role of recombinant allergens – volume: 313 start-page: 514 year: 1996 end-page: 7 article-title: Cohort study of peanut and tree nut sensitisation by age of 4 years publication-title: BMJ – volume: 113 start-page: 141 year: 2004 end-page: 7 article-title: Recombinant lipid transfer protein Cor a 8 from hazelnut publication-title: a new tool for in vitro diagnosis of potentially severe hazelnut allergy – volume: 111 start-page: 889 year: 2003 end-page: 96 article-title: Biological activity of IgE specific for cross‐reactive carbohydrate determinants publication-title: J Allergy Clin Immunol – volume: 112 start-page: 1203 year: 2003 end-page: 7 article-title: Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey publication-title: a 5-year follow-up study – ident: e_1_2_6_3_2 doi: 10.1136/bmj.313.7056.514 – ident: e_1_2_6_39_2 doi: 10.1016/0003-2697(82)90348-7 – ident: e_1_2_6_31_2 doi: 10.1067/mai.2003.173 – ident: e_1_2_6_27_2 doi: 10.1016/0014-5793(93)80641-7 – ident: e_1_2_6_21_2 doi: 10.1111/j.1398-9995.2005.00876.x – volume: 52 start-page: S262 issue: 2 year: 2008 ident: e_1_2_6_26_2 article-title: Expression and characterization of three important panallergens 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Background
Plant food allergy in the Mediterranean area is mainly caused by non‐specific lipid transfer proteins (nsLTP). The aim of this study was to... Background Plant food allergy in the Mediterranean area is mainly caused by non‐specific lipid transfer proteins (nsLTP). The aim of this study was to... Plant food allergy in the Mediterranean area is mainly caused by non-specific lipid transfer proteins (nsLTP). The aim of this study was to characterize peanut... SummaryBackgroundPlant food allergy in the Mediterranean area is mainly caused by non-specific lipid transfer proteins (nsLTP). The aim of this study was to... |
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| SubjectTerms | Allergens - chemistry Allergens - immunology Allergens - pharmacology Allergic diseases Animals Antigens, Plant - chemistry Antigens, Plant - immunology Antigens, Plant - pharmacology Ara h 9 Arachis hypogaea Basophils - immunology Biological and medical sciences Carrier Proteins - chemistry Carrier Proteins - immunology Carrier Proteins - pharmacology Circular Dichroism Digestive allergic diseases Female food allergy Fundamental and applied biological sciences. Psychology Fundamental immunology Glycoproteins - chemistry Glycoproteins - immunology Glycoproteins - pharmacology Histamine - immunology Humans Immunoglobulin E - blood Immunoglobulin E - immunology Immunopathology lipid transfer protein Male Medical sciences peanut allergen Peanut Hypersensitivity - blood Peanut Hypersensitivity - immunology Pichia pastoris Plant Proteins - chemistry Plant Proteins - immunology Plant Proteins - pharmacology Protein Isoforms - chemistry Protein Isoforms - immunology Protein Isoforms - pharmacology Protein Structure, Secondary Pru p 3 Prunus Rabbits Recombinant Proteins - chemistry Recombinant Proteins - immunology Recombinant Proteins - pharmacology Spain Structural Homology, Protein |
| Title | The non-specific lipid transfer protein, Ara h 9, is an important allergen in peanut |
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