Cited by 54

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Molecular approach to a patient’s tailored diagnosis of the oral allergy syndrome

Alessandri, Claudia, Ferrara, Rosetta, Bernardi, Maria Livia, Zennaro, Danila, Tuppo, Lisa, Giangrieco, Ivana, Ricciardi, Teresa, Tamburrini, Maurizio, Ciardiello, Maria Antonietta, Mari, Adriano·2020·Clinical and Translational Allergy

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1186/s13601-020-00329-8

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Figures

Fig. 1 Overview of the relationships between OAS, PFAS, class 1 and class 2 food allergens
Fig. 1 Overview of the relationships between OAS, PFAS, class 1 and class 2 food allergensCC BY · PubMed Central
Fig. 2 Comparison of amino acid sequence identity percentage between different allergens. Bar colors highlight the plant source of allergens, namely green, brown, yellow, red and light grey are for pollen, seed, fruit, root and latex, respectively. The similarity searches were performed with the Allergome Aligner tool, using the Blast algorithm on the Allergome platform (https://www.allergome.org). The amino acid sequence of Bet v 1.0101 (b and c), Bet v 2.0101 (a) and Cry j GRP (d) were used as query sequences. The allergens shown in a and b were selected as representative of the large number of homologs found in the database. When many homologs were found, that giving the highest identity with the query sequence was selected and shown in the figure. c represents a representative selection of Bet v 1 isoallergens/isoforms found in the Allergome database. The sequence identity values of GRP (d) were obtained with the algorithm CLUSTALO on the Uniprot website (https://www.uniprot.org) and they are referred to mature proteins lacking the signal peptide. Cup s 7 was not included because its complete sequence was not available. Additional details on the allergens shown in the Figure are reported in Additional file 1: Tables S1, S2, S3 and S4
Fig. 2 Comparison of amino acid sequence identity percentage between different allergens. Bar colors highlight the plant source of allergens, namely green, brown, yellow, red and light grey are for pollen, seed, fruit, root and latex, respectively. The similarity searches were performed with the Allergome Aligner tool, using the Blast algorithm on the Allergome platform (https://www.allergome.org). The amino acid sequence of Bet v 1.0101 (b and c), Bet v 2.0101 (a) and Cry j GRP (d) were used as query sequences. The allergens shown in a and b were selected as representative of the large number of homologs found in the database. When many homologs were found, that giving the highest identity with the query sequence was selected and shown in the figure. c represents a representative selection of Bet v 1 isoallergens/isoforms found in the Allergome database. The sequence identity values of GRP (d) were obtained with the algorithm CLUSTALO on the Uniprot website (https://www.uniprot.org) and they are referred to mature proteins lacking the signal peptide. Cup s 7 was not included because its complete sequence was not available. Additional details on the allergens shown in the Figure are reported in Additional file 1: Tables S1, S2, S3 and S4CC BY · PubMed Central
Fig. 3 Schematic representation of cross-reactivity occurring between profilins (upper O-ring) and between Bet v 1-related allergenic proteins (lower O-ring) contained in pollens and plant foods. Red and green lines connecting allergy sources indicate single and double cross-reaction relationships, respectively. Arrowheads indicate the direction of data collection. The two pictures were generated on January 2020 by the Allergome software which uses information contained in the own database [53] (https://www.allergome.org)
Fig. 3 Schematic representation of cross-reactivity occurring between profilins (upper O-ring) and between Bet v 1-related allergenic proteins (lower O-ring) contained in pollens and plant foods. Red and green lines connecting allergy sources indicate single and double cross-reaction relationships, respectively. Arrowheads indicate the direction of data collection. The two pictures were generated on January 2020 by the Allergome software which uses information contained in the own database [53] (https://www.allergome.org)CC BY · PubMed Central
Fig. 4 Schematic representation of the class 1 plant food allergens that may cause OAS and/or trigger allergic reactions in other organs and apparatus. These allergens may even induce severe anaphylaxis
Fig. 4 Schematic representation of the class 1 plant food allergens that may cause OAS and/or trigger allergic reactions in other organs and apparatus. These allergens may even induce severe anaphylaxisCC BY · PubMed Central
Fig. 5 Sensitizations detected in 39 patients IgE-positive to at least one of the three analyzed GRP. The columns indicate, in order, patients sensitized to all the three GRP, those bi-sensitized to Cup s 7 and Pru p 3, to Cup s 7 and Pun g 7, to Pru p 7 and Pun g 7 and those monosensitized to Cup s 7, to Pru p 7 and to Pun g 7
Fig. 5 Sensitizations detected in 39 patients IgE-positive to at least one of the three analyzed GRP. The columns indicate, in order, patients sensitized to all the three GRP, those bi-sensitized to Cup s 7 and Pru p 3, to Cup s 7 and Pun g 7, to Pru p 7 and Pun g 7 and those monosensitized to Cup s 7, to Pru p 7 and to Pun g 7CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 1 references

Research works printed but not linked: 135

  1. Mari A, Ballmer-Weber BK, Vieths S. The oral allergy syndrome: improved diagnostic and treatment methods. Curr Opin Allergy Clin Immunol. 2005;5(3):267–73. · DOI
  2. Tuft L, Blumstein GI. Studies in food allergy: II. Sensitization to fresh fruits: clinical and experimental observations. J Allergy. 1942;13(6):574–82. · DOI
  3. Amlot P, Kemeny D, Zachary C, Parkes P, Lessof M. Oral allergy syndrome (OAS): symptoms of IgE-mediated hypersensitivity to foods. Clin Allergy. 1987;17(1):33–42. · DOI
  4. Ortolani C, Ispano M, Pastorello E, Bigi A, Ansaloni R. The oral allergy syndrome. Ann Allergy. 1988;61(6 Pt 2):47–52.
  5. Pastorello E, Ortolani C, Farioli L, Pravettoni V, Ispano M, Borga A, et al. Allergenic cross-reactivity among peach, apricot, plum, and cherry in patients with oral allergy syndrome: an in vivo and in vitro study. J Allergy Clin Immunol. 1994;94(4):699–707. · DOI
  6. Tuano K, Davis C. Oral allergy syndrome in shrimp and house dust mite allergies. J Allergy Clin Immunol Pract. 2018;6(6):2163–4. · DOI
  7. Valenta R, Kraft D. Type 1 allergic reactions to plant derived food: a consequence of primary sensitization to pollen allergens. J Allergy Clin Immunol. 1996;97:893–5. · DOI
  8. Mattila P, Joenvaara S, Renkonen J, Toppila-Salmi S, Renkonen R. Allergy as an epithelial barrier disease. Clin Transl Allergy. 2011;1:5. · DOI
  9. Nasidze I, Li J, Quinque D, Tang K, Stoneking M. Global diversity in the human salivary microbiome. Genome Res. 2009;19:636–43. · DOI
  10. Novak N, Haberstok J, Bieber T, Allam J. The immune privilege of the oral mucosa. Trends Mol Med. 2008;14:191–8. · DOI
  11. Santos AF, Du Toit G, O’Rourke C, Becares N, Couto-Francisco N, Radulovic S, et al. Biomarkers of severity and threshold of allergic reactions during oral peanut challenges. J Allergy Clin Immunol. 2020;S0091–6749(20):30490–5.
  12. Deng S, Yin J. Clinical utility of basophil activation test in diagnosis and predicting severity of mugwort pollen-related peach allergy. World Allergy Organ J. 2019;12(6):100043. · DOI
  13. Scala E, Alessandri C, Bernardi ML, Ferrara R, Palazzo P, Pomponi D, et al. Cross-sectional survey on immunoglobulin E reactivity in 23,077 subjects using an allergenic molecule-based microarray detection system. Clin Exp Allergy. 2010;40:911–21. · DOI · Paper page
  14. Pasquariello MS, Palazzo P, Tuppo L, Liso M, Petriccione M, Rega P, et al. Analysis of the potential allergenicity of traditional apple cultivars by Multiplex Biochip-Based Immunoassay. Food Chem. 2012;135(1):219–27. · DOI
  15. Ciardiello MA, Giangrieco I, Tuppo L, Tamburrini M, Buccheri M, Palazzo P, et al. Influence of the natural ripening stage, cold storage, and ethylene treatment on the protein and IgE-binding profiles of green and gold kiwi fruit extracts. J Agric Food Chem. 2009;57(4):1565–71. · DOI
  16. Giangrieco I, Ricciardi T, Alessandri C, Farina L, Crescenzo R, Tuppo L, et al. ENEA, a peach and apricot IgE-binding protein cross-reacting with the latex major allergen Hev b 5. Mol Immunol. 2019;112:347–57. · DOI
  17. Carnés J, Fernández-Caldas E, Gallego MT, Ferrer A, Cuesta-Herranz J. Pru p 3 (LTP) content in peach extracts. Allergy. 2002;57(11):1071–5. · DOI
  18. Ciardiello MA, Tamburrini M, Liso M, Crescenzo R, Rafaiani C, Mari A. Food allergen profiling: a big challenge. Food Res Int. 2013;54(1):1033–41. · DOI
  19. Alessandri C, Ferrara R, Bernardi ML, Zennaro D, Tuppo L, Giangrieco I, et al. Diagnosing allergic sensitizations in the third millennium: why clinicians should know allergen molecule structures. Clin Transl Allergy. 2017;7:21. · DOI
  20. Deinhofer K, Sevcik H, Balic N, Harwanegg C, Hiller R, Rumpold H, et al. Microarrayed allergens for IgE profiling. Methods. 2004;32(3):249–54. · DOI
  21. Heffler E, Puggioni F, Peveri S, Montagni M, Canonica GW, Melioli G. Extended IgE profile based on an allergen macroarray: a novel tool for precision medicine in allergy diagnosis. World Allergy Organ J. 2018;11(1):7. · DOI
  22. Tuppo L, Alessandri C, Pasquariello MS, Petriccione M, Giangrieco I, Tamburrini M, et al. Pomegranate cultivars: identification of the new IgE-binding protein pommaclein and analysis of antioxidant variability. J Agric Food Chem. 2017;65(13):2702–10. · DOI
  23. Tuppo L, Alessandri C, Giangrieco I, Ciancamerla M, Rafaiani C, Tamburrini M, et al. Isolation of cypress gibberellin-regulated protein: analysis of its structural features and IgE binding competition with homologous allergens. Mol Immunol. 2019;114:189–95. · DOI
  24. Tuppo L, Giangrieco I, Alessandri C, Ricciardi T, Rafaiani C, Ciancamerla M, et al. Pomegranate chitinase III: identification of a new allergen and analysis of sensitization patterns to chitinases. Mol Immunol. 2018;103:89–95. · DOI
  25. Santoni M, Ciardiello MA, Zampieri R, Pezzotti M, Giangrieco I, Rafaiani C, et al. Plant-made Bet v 1 for molecular diagnosis. Front Plant Sci. 2019;10:1273. · DOI
  26. Offermann LR, Schlachter CR, Perdue ML, Majorek KA, He JZ, Booth WT, et al. Structural, functional, and immunological characterization of profilin panallergens Amb a 8, Art v 4, and Bet v 2. J Biol Chem. 2016;291(30):15447–59. · DOI
  27. Ladics GS. Assessment of the potential allergenicity of genetically-engineered food crops. J Immunotoxicol. 2019;16(1):43–53. · DOI
  28. Bernardi ML, Giangrieco I, Camardella L, Ferrara R, Palazzo P, Panico MR, et al. Allergenic lipid transfer proteins from plant-derived foods do not immunologically and clinically behave homogeneously: the kiwifruit LTP as a model. PLoS ONE. 2011;6(11):e27856. · DOI
  29. Giangrieco I, Alessandri C, Rafaiani C, Santoro M, Zuzzi S, Tuppo L, et al. Structural features, IgE binding and preliminary clinical findings of the 7 kDa lipid transfer protein from tomato seeds. Mol Immunol. 2015;66(2):154–63. · DOI
  30. Ferreira F, Hirtenlehner K, Jilek A, Godnik-Cvar J, Breiteneder H, Grimm R, et al. Dissection of immunoglobulin E and T lymphocyte reactivity of isoforms of the major birch pollen allergen Bet v 1: potential use of hypoallergenic isoforms for immunotherapy. J Exp Med. 1996;183(2):599–609. · DOI
  31. Chan SK, Pomés A, Hilger C, Davies JM, Mueller G, Kuehn A, et al. Keeping allergen names clear and defined. Front Immunol. 2019;10:2600. · DOI
  32. Mari A, Scala E, Palazzo P, Ridolfi S, Zennaro D, Carabella G. Bioinformatics applied to allergy: allergen databases, from collecting sequence information to data integration. The Allergome platform as a model. Cell Immunol. 2006;244(2):97–100. · DOI
  33. Jimenez-Lopez JC, Rodríguez-García MI, Alché JD. Analysis of the effects of polymorphism on pollen profilin structural functionality and the generation of conformational, T- and B-cell epitopes. PLoS ONE. 2013;8(10):e76066. · DOI
  34. Ferreira F, Ebner C, Kramer B, Casari G, Briza P, Kungl AJ, et al. Modulation of IgE reactivity of allergens by site-directed mutagenesis: potential use of hypoallergenic variants for immunotherapy. FASEB J. 1998;12:231–42. · DOI
  35. Reinmuth-Selzle K, Kampf CJ, Lucas K, Lang-Yona N, Fröhlich-Nowoisky J, Shiraiwa M, et al. Air pollution and climate change effects on allergies in the anthropocene: abundance, interaction, and modification of allergens and adjuvants. Environ Sci Technol. 2017;51(8):4119–41. · DOI
  36. Bublin M, Breiteneder H. Cross-reactivities of non-homologous allergens. Allergy. 2019. https://doi.org/10.1111/all.14120 . · DOI
  37. Bublin M, Kostadinova M, Radauer C, Hafner C, Szépfalusi Z, Varga EM, et al. IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3. J Allergy Clin Immunol. 2013;132(1):118–24. · DOI
  38. Sampson H. Food allergy part 1: immunopathogenesis and clinical disorders. J Allergy Clin Immunol. 1999;103:717–28. · DOI
  39. Breiteneder H, Ebner C. Molecular and biochemical classification of plant-derived food allergens. J Allergy Clin Immunol. 2000;106:27–36. · DOI
  40. Petersen A, Rennert S, Kull S, Becker W, Notbohm H, Goldmann T, et al. Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8. Biol Chem. 2014;395(2):239–50. · DOI
  41. Mittag D, Vieths S, Vogel L, Becker WM, Rihs HP, Helbling A, et al. Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. J Allergy Clin Immunol. 2004;113(1):148–54. · DOI
  42. Skamstrup Hansen V, Vieths S, Vestergaard H, Skov P, Bindslev-Jensen C, Poulsen L. Seasonal variation in food allergy to apple. J Chromatogr B Biomed Sci Appl. 2001;756:19–32. · DOI
  43. Carlson G, Coop C. Pollen food allergy syndrome (PFAS): a review of current available literature. Ann Allergy Asthma Immunol. 2019;123(4):359–65. · DOI · Paper page
  44. Aalberse RC. Assessment of allergen cross-reactivity. Clin Mol Allergy. 2007;5:2. · DOI
  45. Paulus KE, Schmid B, Zajic D, Schäfer A, Mahler V, Sonnewald U. Hypoallergenic profilin—a new way to identify allergenic determinants. FEBS J. 2012;279(15):2727–36. · DOI
  46. Wagner S, Radauer C, Bublin M, Hoffmann-Sommergruber K, Kopp T, Greisenegger EK, et al. Naturally occurring hypoallergenic Bet v 1 isoforms fail to induce IgE responses in individuals with birch pollen allergy. J Allergy Clin Immunol. 2008;121(1):246–52. · DOI
  47. Jimenez-Lopez JC, Morales S, Castro AJ, Volkmann D, Rodríguez-García MI, de Alché JD. Characterization of profilin polymorphism in pollen with a focus on multifunctionality. PLoS ONE. 2012;7(2):e30878. · DOI
  48. Abedini S, Sankian M, Falak R, Tehrani M, Talebi F, Shirazi F, et al. An approach for detection and quantification of fruits’ natural profilin: natural melon profilin as a model. Food Agric Immunol. 2011;22:47–55. · DOI
  49. Sun T, Li S, Ren H. Profilin as a regulator of the membrane-actin cytoskeleton interface in plant cells. Front Plant Sci. 2013;4:512. · DOI
  50. Kapingidza AB, Pye SE, Hyduke N, Dolamore C, Pote S, Schlachter CR, et al. Comparative structural and thermal stability studies of Cuc m 2.0101, Art v 4.0101 and other allergenic profilins. Mol Immunol. 2019;114:19–29. · DOI · Paper page
  51. Chruszcz M, Kapingidza AB, Dolamore C, Kowal K. A robust method for the estimation and visualization of IgE cross-reactivity likelihood between allergens belonging to the same protein family. PLoS ONE. 2018;13(11):e0208276. · DOI
  52. Mari A. Multiple pollen sensitization: a molecular approach to the diagnosis. Int Arch Allergy Immunol. 2001;125:57–65. · DOI
  53. Elfman L, Svensson M, Lidholm J, Pauli G, Valenta R. Different profiles in specific IgE to rBet v 1 and rBet v 2 in patients allergic to birch pollen from six countries. Int Arch Allergy Immunol. 1997;113:249–51. · DOI
  54. Pauli G, Oster J, Deviller P, Heiss S, Bessot J, Susani M, et al. Skin testing with recombinant allergens rBet v 1 and birch profilin, rBet v 2: diagnostic value for birch pollen and associated allergies. J Allergy Clin Immunol. 1996;97:1100–9. · DOI
  55. Tavares B, Machado D, Loureiro G, Cemlyn-Jones J, Pereira C. Sensitization to profilin in the Central region of Portugal. Sci Total Environ. 2008;407:273–8. · DOI
  56. Asero R, Monsalve R, Barber D. Profilin sensitization detected in the office by skin prick test: a study of prevalence and clinical relevance of profilin as a plant food allergen. Clin Exp Allergy. 2008;38:1033–7. · DOI
  57. Alvarado M, Jimeno L, De La Torre F, Boissy P, Rivas B, Lazaro M, et al. Profilin as a severe food allergen in allergic patients overexposed to grass pollen. Allergy. 2014;69:1610–6. · DOI · Paper page
  58. Van Ree R, Voitenko V, van Leeuwen A, Aalberse RC. Profilin is a cross-reactive allergen in pollen and vegetable foods. Int Arch Allergy Immunol. 1992;98:97–104. · DOI
  59. Vallier P, Ballard S, Harf R, Valenta R, Deviller P. Identification of profilin as an IgE-binding component in latex from Hevea brasiliensis: clinical implications. Clin Exp Allergy. 1995;25:332–9. · DOI
  60. Asero R, Mistrello G, Roncarolo D, Amato S, Zanoni D, Barocci F, et al. Detection of clinical markers of sensitization to profilin in patients allergic to plant derived foods. J Allergy Clin Immunol. 2003;112:427–32. · DOI
  61. Cuesta-Herranz C, Pastor C, Figueredo E, Vidarte L, De Las Heras M, Duran C, et al. Identification of Cucumisin (Cuc m 1), a subtilisin-like endopeptidase, as the major allergen of melon fruit. Clin Exp Allergy. 2003;33:827–33. · DOI
  62. Fah J, Wuthrich B, Vieths S. Anaphylactic reaction to lychee fruit: evidence for sensitization to profilin. Clin Exp Allergy. 1995;25:1018–23. · DOI
  63. Reindl J, Anliker M, Karamloo F, Vieths S, Wuthrich B. Allergy caused by ingestion of zucchini (Cucurbita pepo): characterization of allergens and cross-reactivity to pollen and other foods. J Allergy Clin Immunol. 2000;106:379–85. · DOI
  64. Pastorello E, Farioli L, Pravettoni V, Scibilia J, Mascheri A, Borgonovo L, et al. Pru p 3-sensitised Italian peach-allergic patients are less likely to develop severe symptoms when also presenting IgE antibodies to Pru p 1 and Pru p 4. Int Arch Allergy Immunol. 2011;156:362–72. · DOI
  65. Scala E, Abeni D, Guerra E, Locanto M, Pirrotta L, Meneguzzi G, et al. Co-sensitization to profilin is associated with less severe reactions to foods in nsLTPs- and storage proteins-reactors and with less severe respiratory allergy. Allergy. 2018;73:1921–3. · DOI
  66. Asaumi T, Sato S, Yanagida N, Takahashi K, Mori Y, Okazaki F, et al. IgE-specific Pru p 4 negatively predicts systemic allergy reaction to peach among Japanese children. Allergol Int. 2019;68:546–8. · DOI
  67. Radauer C, Breiteneder H. Evolutionary biology of plant food allergens. J Allergy Clin Immunol. 2007;120:518–25. · DOI
  68. D’Avino R, Bernardi ML, Wallner M, Palazzo P, Camardella L, Tuppo L, et al. Kiwifruit Act d 11 is the first member of the ripening-related protein family identified as an allergen. Allergy. 2011;66(7):870–7. · DOI
  69. Chruszcz M, Ciardiello MA, Osinski T, Majorek KA, Giangrieco I, Font J, et al. Structural and bioinformatic analysis of the kiwifruit allergen Act d 11, a member of the family of ripening-related proteins. Mol Immunol. 2013;56(4):794–803. · DOI
  70. Guhsl E, Hofstetter G, Hemmer W, Ebner C, Vieths S, Vogel L, et al. Vig R 6, the cytokinin-specific binding protein from mung bean (Vigna Radiata) sprouts, cross-reacts with Bet v 1-related allergens and binds IgE from birch pollen allergic patients’ Sera. Mol Nutr Food Res. 2014;58:625–34. · DOI
  71. Sancho A, Wangorsch A, Jensen B, Watson A, Alexeev Y, Johnson P, et al. Responsiveness of the major birch allergen Bet v 1 scaffold to the gastric environment: impact on structure and allergenic activity. Mol Nutr Food Res. 2011;55:1690–9. · DOI
  72. Pekar J, Ret D, Untersmayr E. Stability of allergens. Mol Immunol. 2018;100:14–20. · DOI · Paper page
  73. Franz-Oberdorf K, Eberlein B, Edelmann K, Hücherig S, Besbes F, Darsow U, et al. Fra a 1.02 is the most potent isoform of the Bet v 1-like allergen in strawberry fruit. J Agric Food Chem. 2016;64(18):3688–96. · DOI
  74. van Rhijn B, van Ree R, Versteeg S, Vlieg-Boerstra B, Sprikkelman A, Terreehorst I, et al. Birch pollen sensitization with cross-reactivity to food allergens predominates in adults with eosinophilic esophagitis. Allergy. 2013;68:1475–81. · DOI
  75. Moneo I, Gómez M, Sánchez-Monge R, Alday E, de las Heras M, Esteban I, et al. Lack of crossreaction with Bet v 1 in patients sensitized to Dau c 1, a carrot allergen. Ann Allergy Asthma Immunol. 1999;83:71–5. · DOI
  76. Blankestijn MA, Knulst AC, Knol EF, et al. Sensitization to PR-10 proteins is indicative of distinctive sensitization patterns in adults with a suspected food allergy. Clin Transl Allergy. 2017;7:42. · DOI
  77. Gepp B, Lengger N, Bublin M, Hemmer W, Breiteneder H, Radauer C. Chimeras of Bet v 1 and Api g 1 reveal heterogeneous IgE responses in patients with birch pollen allergy. J Allergy Clin Immunol. 2014;134:188–94. · DOI
  78. Hauser M, Asam C, Himly M, Palazzo P, Voltolini S, Montanari C, et al. Bet v 1-like pollen allergens of multiple fagales species can sensitize atopic individuals. Clin Exp Allergy. 2011;41:1804–14. · DOI
  79. Rashid R, Smith K, Nambiar K, Frew A, Tarzi M. Pollen-food syndrome is related to Bet v 1/PR-10 protein sensitisation, but not all patients have spring rhinitis. Allergy. 2011;66:1391–2. · DOI
  80. Berneder M, Bublin M, Hoffmann-Sommergruber K, Hawranek T, Lang R. Allergen chip diagnosis for soy-allergic patients: Gly m 4 as a marker for severe food-allergic reactions to soy. Int Arch Allergy Immunol. 2013;161:229–33. · DOI
  81. Ballmer-Weber B, Vieths S, Luttkopf D, Heuschmann P, Wuthrich B. Celery allergy confirmed by double-blind, placebo-controlled food challenge: a clinical study in 32 subjects with a history of adverse reactions to celery root. J Allergy Clin Immunol. 2000;106:373–8. · DOI
  82. Ballmer-Weber B, Wuthrich B, Wangorsch A, Fotisch K, Altmann F, Vieths S. Carrot allergy: double-blinded, placebo-controlled food challenge and identification of the allergens. J Allergy Clin Immunol. 2001;108:301–7. · DOI
  83. Bolhaar S, Van Ree R, Bruijnzeel-Koomen C, Knulst A, Zuidmeer L. Allergy to jackfruit: a novel example of Bet v 1-related food allergy. Allergy. 2004;59:1187–92. · DOI
  84. Bolhaar S, van Ree R, Ma Y, Bruijnzeel-Koomen C, Vieths S, HoffmannSommergruber K, et al. Severe allergy to sharon fruit caused by birch pollen. Int Arch Allergy Immunol. 2005;136:45–52. · DOI
  85. Asero R, Celi G, Scala E. Labile plant food allergens: Really so harmless? Case series and literature review. Allergy. 2020;17 (Online ahead of print). · DOI
  86. Krause S, Reese G, Randow S, Zennaro D, Quaratino D, Palazzo P, et al. Lipid transfer protein (Ara h 9) as a new peanut allergen relevant for a Mediterranean allergic population. J Allergy Clin Immunol. 2009;124(4):771–8. · DOI
  87. Andersen MBS, Hall S, Dragsted LO. Identification of European allergy patterns to the allergen families PR-10, LTP, and profilin from Rosaceae fruits. Clin Rev Allergy Immunol. 2011;41(1):4–19. · DOI · Paper page
  88. Elisyutina O, Fedenko E, Campana R, Litovkina A, Ilina N, Kudlay D, et al. Bet v 1-specific IgE levels and PR-10 reactivity discriminate silent sensitization from phenotypes of birch allergy. Allergy. 2019;74:2525–8. · DOI
  89. Scheurer S, Schülke S. Interaction of non-specific lipid-transfer proteins with plant-derived lipids and its impact on allergic sensitization. Front Immunol. 2018;9:1389. · DOI
  90. Dubiela P, Aina R, Polak D, Geiselhart S, Humeniuk P, Bohle B, et al. Enhanced Pru p 3 IgE-binding activity by selective free fatty acid-interaction. J Allergy Clin Immunol. 2017;140(6):1728–31. · DOI
  91. Wildner S, Griessner I, Stemeseder T, Regl C, Soh W, Stock L, et al. Boiling down the cysteine-stabilized LTP Fold—loss of structural and immunological integrity of allergenic Art v 3 and Pru P 3 as a consequence of irreversible lanthionine formation. Mol Immunol. 2019;116:140–50. · DOI
  92. Gaier S, Marsh J, Oberhuber C, Rigby NM, Lovegrove A, Alessandri S, et al. Purification and structural stability of the peach allergens Pru p 1 and Pru p 3. Mol Nutr Food Res. 2008;52(2):S220–9.
  93. Pastorello E, Farioli L, Pravettoni V, Ortolani C, Ispano M, Monza M. The major allergen of peach (Prunus persica) is a lipid transfer protein. J Allergy Clin Immunol. 1999;103:520–6. · DOI
  94. Barber D, de la Torre F, Lombardero M, Antepara I, Colas C, et al. Component-resolved diagnosis of pollen allergy based on skin testing with profilin, polcalcin and lipid transfer protein pan-allergens. Clin Exp Allergy. 2009;39:1764–73. · DOI
  95. Gao Z, Yang Z, Wu S, Wang H, Liu M, Mao W, et al. Peach allergy in China: a dominant role for mugwort pollen lipid transfer protein as a primary sensitizer. J Allergy Clin Immunol. 2013;131:224–6. · DOI
  96. Murad A, Katelaris C, Baumgart K. A case study of apple seed and grape allergy with sensitisation to nonspecific lipid transfer protein. Asia Pac Allergy. 2016;6:129–32. · DOI
  97. Mothes-Luksch N, Raith M, Stingl G, et al. Pru p 3, a marker allergen for lipid transfer protein sensitization also in Central Europe. Allergy. 2017;72:1415–8. · DOI
  98. Bolla M, Zenoni S, Scheurer S, Vieths S, San Miguel Moncin MEM, Olivieri M, et al. Pomegranate (Punica granatum L.) expresses several nsLTP isoforms characterized by different immunoglobulin E-binding properties. Int Arch Allergy Immunol. 2014;164(2):112–21. · DOI
  99. Rodrigues-Alves R, Lopez A, Pereira-Santos MC, Lopes-Silva S, Spinola-Santos A, Costa C, Branco-Ferreira M, Lidholm J, Pereira-Barbosa M. Clinical, anamnestic and serological features of peach allergy in Portugal. Int Arch Allergy Immunol. 2009;149:65–73. · DOI
  100. Asero R, Piantanida M, Pinter E, Pravettoni V. The clinical relevance of lipid transfer protein. Clin Exp Allergy. 2018;48(1):6–12. · DOI
  101. Brenna O, Pastorello E, Farioli L, Pravettoni V, Pompei C. Presence of allergenic proteins in different peach (Prunus persica) cultivars and dependence of their content on fruit ripening. J Agric Food Chem. 2004;52:7997–8000. · DOI
  102. Pascal M, Munoz-Cano R, Milà J, Sanz M, Diaz-Perales A, Sánchez-López J, et al. Nonsteroidal anti-inflammatory drugs enhance IgE-mediated activation of human basophils in patients with food anaphylaxis dependent on and independent of nonsteroidal anti-inflammatory drugs. Clin Exp Allergy. 2016;46:1111–9. · DOI
  103. Romano A, Scala E, Rumi G, Gaeta F, Caruso C, Alonzi C, et al. Lipid transfer proteins: the most frequent sensitizer in Italian subjects with food-dependent exercise-induced anaphylaxis. Clin Exp Allergy. 2012;42:1643–53. · DOI
  104. Tordesillas L, Sirvent S, Diaz-Perales A, Villalba M, Cuesta-Herranz J, Rodriguez R, et al. Plant lipid transfer protein allergens: no cross-reactivity between those from foods and olive and Parietaria pollen. Int Arch Allergy Immunol. 2011;156:291–6. · DOI
  105. Pastorello E, Pravettoni V, Farioli L, Rivolta F, Conti A, Ispano M, et al. Hypersensitivity to mugwort (Artemisia vulgaris) in patients with peach allergy is due to a common lipid transfer protein allergen and is often without clinical expression. J Allergy Clin Immunol. 2002;110(2):310–7. · DOI
  106. Deng S, Yin J. Mugwort pollen-related food allergy: lipid transfer protein sensitization and correlation with the severity of allergic reactions in a Chinese population. Allergy Asthma Immunol Res. 2019;11:116–28. · DOI · Paper page
  107. Gadermaier G, Hauser M, Egger M, Ferrara R, Briza P, Souza Santos K, et al. Sensitization prevalence, antibody cross-reactivity and immunogenic peptide profile of Api g 2, the non-specific lipid transfer protein 1 of celery. PLoS ONE. 2011;6(9):e24150. · DOI
  108. Lauer I, Miguel-Moncin M, Abel T, Foetisch K, Hartz C, Fortunato D. 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. · DOI
  109. Wangorsch A, Larsson H, Messmer M, García-Moral A, Lauer I, Wolfheimer S, et al. Molecular cloning of plane pollen allergen Pla a 3 and its utility as diagnostic marker for peach associated plane pollen allergy. Clin Exp Allergy. 2016;46:764–74. · DOI
  110. Oeo-Santos C, Navas A, Benedé S, Ruíz-León B, Díaz-Perales A, Vogel L, et al. New insights into the sensitization to nonrelated nsLTPs from pollen and food: new role of the allergen Ole e 7. Allergy. 2020;75(4):798–807. · DOI
  111. Bousquet J, Anto J, Bachert C, Bousquet P, Colombo P, Crameri R, et al. Factors responsible for differences between asymptomatic subjects and patients presenting an IgE sensitization to allergens. A GA2LEN project. Allergy. 2006;61:671–80. · DOI
  112. Skypala I, Cecchi L, Shamji M, Scala E, Till S. Lipid transfer protein allergy in the United Kingdom; 2019, characterisation and comparison with a matched Italian cohort. Allergy. 2019;74:1340–51. · DOI
  113. Ma S, Yin J, Jiang N. Component-resolved diagnosis of peach allergy and its relationship with prevalent allergenic pollens in china. J Allergy Clin Immunol. 2013;132:764–7. · DOI
  114. Tuppo L, Alessandri C, Pomponi D, Picone D, Tamburrini M, Ferrara R, et al. Peamaclein—a new peach allergenic protein: similarities, differences and misleading features compared to Pru p 3. Clin Exp Allergy. 2013;43(1):128–40. · DOI
  115. Tuppo L, Spadaccini R, Alessandri C, Wienk H, Boelens R, Giangrieco I, et al. Structure, stability, and IgE binding of the peach allergen Peamaclein (Pru p 7). Biopolymers. 2014;102(5):416–25. · DOI
  116. Inomata N, Miyakawa M, Ikeda N, Oda K, Aihara M. Identification of gibberellin-regulated protein as a new allergen in orange allergy. Clin Exp Allergy. 2018;48(11):1509–20. · DOI
  117. Camara MCVL, Rodrigues C, de Oliveira J, Faulds C, Bertrand E, et al. Current advances in gibberellic acid (GA3) production, patented Technologies and Potential Applications. Planta. 2018;248:1049–62. · DOI
  118. Sénéchal HŠJ, Melčová M, et al. A new allergen family involved in pollen food-associated syndrome: snakin/gibberellin-regulated proteins. J Allergy Clin Immunol. 2018;141(411–4):e4.
  119. Poncet P, Aizawa T, Sénéchal H. The subtype of Cupressaceae pollinosis associated with Pru p 7 sensitization is characterized by a sensitization to a cross-reactive gibberellin-regulated protein in cypress pollen: BP14. Clin Exp Allergy. 2019;49(8):1163–6. · DOI
  120. Shahali Y, Sutra J, Charpin D, Mari A, Guilloux L, Senechal H, et al. Differential IgE sensitization to cypress pollen associated to a basic allergen of 14 kDa. FEBS J. 2012;279:1445–55. · DOI
  121. Klingebiel C, Chantran Y, Arif-Lusson R, Ehrenberg A, Ostling J, Poisson A, et al. Pru p 7 sensitisation is a predominant cause of severe, cypress pollen-associated peach allergy. Clin Exp Allergy. 2019;49:526–36. · DOI
  122. Charpin D, Pichot C, Belmonte J, Sutra J, Zidkova J, Chanez P, et al. Cypress pollinosis: from tree to clinic. Clin Rev Allergy Immunol. 2017;56:174–95. · DOI · Paper page
  123. Wagner S, Breiteneder H. Latex-fruit syndrome. Biochem Soc Trans. 2002;30:935–40. · DOI
  124. Garcia Ortiz J, Moyano J, Alvarez M, Bellido J. Latex allergy in fruit-allergic patients. Allergy. 1998;53:532–6. · DOI
  125. Sinha M, Singh R, Kushwaha G, Iqbal N, Singh A, Kaushik S, et al. Current overview of allergens of plant pathogenesis related protein families. Sci World J. 2014;2014:543195.
  126. Wagner SRC, Hafner C, Fuchs H, Jensen-Jarolim E, Wuthrich B, Scheiner O, Breiteneder H. Molecular characterization of recombinant mus a 5 allergen from banana fruit. Clin Exp Allergy. 2014;34:1739–46. · DOI
  127. Palomares O, Villalba M, Quiralte J, Polo F, Rodriguez R. 1,3-beta-glucanases as candidates in latex-pollen-vegetable food cross-reactivity. Clin Exp Allergy. 2005;35:345–51. · DOI
  128. Taira THH, Tajiri Y, Onaga S, Uechi G, Iwasaki H, Ohnuma T, Fukamizo T. A plant class V chitinase from a cycad (Cycas revoluta): biochemical characterization, cDNA isolation, and posttranslational modification. Glycobiology. 2009;19:1452–61. · DOI
  129. Sanchez-Monge R, Blanco C, Perales A, Collada C, Carrillo T, Aragoncillo C, et al. Class I chitinases, the panallergens responsible for the latex-fruit syndrome, are induced by ethylene treatment and inactivated by heating. J Allergy Clin Immunol. 2000;106:190–5. · DOI
  130. Blanco C, Diaz-Perales A, Collada C, Sánchez-Monge R, Aragoncillo C, Castillo R, et al. Class I chitinases as potential panallergens involved in the latex-fruit syndrome. J Allergy Clin Immunol. 1999;103:507–13. · DOI
  131. Radauer C, Adhami F, Furtler I, Wagner S, Allwardt D, Scala E, et al. Latex-allergic patients sensitized to the major allergen hevein and hevein-like domains of class I chitinases show no increased frequency of latex-associated plant food allergy. Mol Immunol. 2011;48:600–9. · DOI
  132. Lee M, Hwang G, Chen Y, Lin H, Wu C. Molecular cloning of Indian jujube (Zizyphus mauritiana) allergen Ziz m 1 with sequence similarity to plant class III chitinases. Mol Immunol. 2006;43:1144–51. · DOI
  133. Marzban G, Herndl A, Kolarich D, Maghuly F, Mansfeld A, Hemmer W, et al. Identification of four IgE-reactive proteins in raspberry (Rubus ideaeus L.). Mol Nutr Food Res. 2008;52:1497–506. · DOI
  134. Santos KS, Gadermaier G, Vejvar E, Arcuri HA, Galvão CE, Yang AC, et al. Novel allergens from ancient foods: Man e 5 from manioc (Manihot esculenta Crantz) cross reacts with Hev b 5 from latex. Mol Nutr Food Res. 2013;57(6):1100–9. · DOI
  135. Tomas-Perez M, Hernández-Martín I, de Fernández Alba-Porcel I, Pagola M, Carretero P, Dominguez-Ortega J, et al. Allergy to vegetables belonging to the Solanaceae family. Rev Alerg Mex. 2019;66:322–8. · DOI

Cited by

Sorted by citations

See all 54

Metadata

Authors
Alessandri, C., Ferrara, R., Bernardi, M. L., Zennaro, D., Tuppo, L., Giangrieco, I., Ricciardi, T., Tamburrini, M., Ciardiello, M. A., & Mari, A.
Venue
Clinical and Translational Allergy
Publisher
Wiley
Published
2020-06-17
Volume
10
Issue
1
ISSN
2045-7022
Cited by
54
References
1
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Molecular approach to a patient’s tailored diagnosis of the oral allergy syndrome. https://app.cochat.ai/papers/10.1186/s13601-020-00329-8
The paper
Alessandri, C., Ferrara, R., Bernardi, M. L., Zennaro, D., Tuppo, L., Giangrieco, I., Ricciardi, T., Tamburrini, M., Ciardiello, M. A., & Mari, A. (2020). Molecular approach to a patient’s tailored diagnosis of the oral allergy syndrome. Clinical and Translational Allergy. https://doi.org/10.1186/s13601-020-00329-8