Current Allergy and Asthma Reports

, Volume 4, Issue 5, pp 401–408

Cross-reactivity of pollen allergens

  • Richard W. Weber
Article

Abstract

Pollen cross-allergenicity has practical implications on the management of inhalant allergy, in both evaluation and therapy, especially with allergen vaccine immunotherapy. The study of cross-reactivity among pollen allergens has expanded beyond investigation of crude extracts to the characterization and cloning of numerous pollen proteins. In this review, the interrelationships between these pollen allergens in the context of botanical systematics are examined, to provide a framework for cross-reactivity understanding. Recommendations for choices in evaluation and therapy are given.

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References and Recommended Reading

  1. 1.
    Breiteneder H, Radauer C: A classification of plant food allergens. J Allergy Clin Immunol 2004, 113:821–830. This is an excellent current review of several classes of plant allergens that addresses the function of the proteins and, thus, their likelihood of being found in pollen proteins.PubMedCrossRefGoogle Scholar
  2. 2.
    Judd WS, Campbell CS, Kellogg EA, Stevens PF: Plant systematics: a phylogenetic approach.Snderland, MA: Sinauer Associates; 1999. This is a superb reference text for those interested in the foundations of present plant systematics.Google Scholar
  3. 3.
    Weber RW: Cross-reactivity of plant and animal allergens. Clin Rev Allergy Immunol 2001, 21:153–202. This review covers, in great detail, historic studies as well as recent (up to 2001) research on pollen allergen cross-reactivity. Fungal, inhalant animal, and venom allergens are addressed as well.PubMedCrossRefGoogle Scholar
  4. 4.
    Schwietz LA, Goetz DW, Whisman BA, Reid MJ: Crossreactivity among conifer pollens. Ann Allergy Asthma Immunol 2000, 84:87–93.PubMedGoogle Scholar
  5. 5.
    Midoro-Horiuti T, Goldblum RM, Kurosky A, et al.: Molecular cloning of the mountain cedar (Juniperus ashei) pollen major allergen, Jun a 1. J Allergy Clin Immunol 1999, 104:613–617.PubMedCrossRefGoogle Scholar
  6. 6.
    Canini A, Giovinazzi J, Iacovacci P, et al.: Localisation of a carbohydrate epitope recognised by human IgE in pollen of Cupressaceae. J Plant Res 2004, 11:147–153.CrossRefGoogle Scholar
  7. 7.
    van Ree R: Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases. Int Arch Allergy Immunol 2002, 129:189–197.PubMedCrossRefGoogle Scholar
  8. 8.
    Tinghino R, Barletta B, Palumbo S, et al.: Molecular characterization of a cross-reactive Juniperus oxycedrus pollen allergen, Jun o 2: a novel calcium-binding allergen. J Allergy Clin Immunol 1998, 101:772–777.PubMedCrossRefGoogle Scholar
  9. 9.
    Midoro-Horiuti T, Mathura V, Schein CH, et al.: Major linear IgE epitopes of mountain cedar pollen allergen Jun a 1 map to the pectate lysate catalytic site. Mol Immunol 2003, 40:555–562. This is a fine example of characterization of a major allergen group, providing insight into the reason for its ubiquitous nature within Cupressaceae.PubMedCrossRefGoogle Scholar
  10. 10.
    Andersson K, Lidholm J: Characteristics and immunobiology of grass pollen allergens. Int Arch Allergy Immunol 2003, 130:87–107. This paper is a thorough and up-to-date review of the ten defined grass pollen allergen groups. More than any other recent review, this paper provides an excellent reference source for understanding these allergens.PubMedCrossRefGoogle Scholar
  11. 11.
    Fahlbusch B, Müller W-D, Rudeschko O, et al.: Detection and quantification of group 4 allergens in grass pollen extracts using monoclonal antibodies. Clin Exp Allergy 1998, 28:799–807.PubMedCrossRefGoogle Scholar
  12. 12.
    Grobe K, Becker W-M, Schlaak M, Petersen A: Grass group I allergens (beta-expansins) are novel, papain-related proteinases. Eur J Biochem 1999, 263:33–40.PubMedCrossRefGoogle Scholar
  13. 13.
    Weber RW: Patterns of pollen cross-allergenicity. J Allergy Clin Immunol 2003, 112:229–239. This review provides a detailed discussion of recent advances in pollen cross-reactivity.PubMedCrossRefGoogle Scholar
  14. 14.
    van Ree R, van Leeuwen WA, van den Berg M, et al.: IgE and IgG cross-reactivity among Lol p I and Lol p II/III: identification of the C-termini of Lol p I, II, and III as cross-reactive structures. Allergy 1994, 49:254–261.PubMedCrossRefGoogle Scholar
  15. 15.
    Gavrovic-Jankulovic M, Cirkovic T, Burazer L, et al.: IgE cross-reactivity between meadow fescue pollen and kiwi fruit in patients’ sera with sensitivity to both extracts. J Investig Allergol Clin Immunol 2002, 12:279–286.PubMedGoogle Scholar
  16. 16.
    Fahlbusch B, Müller W-D, Diener C, Jäger L: Detection of cross reactive determinants in grass pollen extracts using monoclonal antibodies against group IV and group V allergens. Clin Exp Allergy 1993, 23:51–60.PubMedCrossRefGoogle Scholar
  17. 17.
    Müller W-D, Karamfilov T, Bufe A, et al.: Group 5 allergens of timothy grass (Phl p 5) bear cross-reacting T cell epitopes with group 1 allergens of rye grass (Lol p 1). Int Arch Allergy Immunol 1996, 109:352–355.PubMedGoogle Scholar
  18. 18.
    Matthiesen F, Schumacher MJ, Løwenstein H: Characterization of the major allergen of Cynodon dactylon (Bermuda grass) pollen, Cyn d I. J Allergy Clin Immunol 1991, 88:763–774.PubMedCrossRefGoogle Scholar
  19. 19.
    Chang ZN, Liu CC, Perng HC, et al.: A common allergic epitope of Bermuda grass pollen shared with other grass pollens. J Biomed Sci 1994, 1:93–99.PubMedCrossRefGoogle Scholar
  20. 20.
    Smith PM, Ong EK, Knox RB, Singh MB: Immunological relationships among group I and group V allergens from grass pollens. Mol Immunol 1994, 31:491–498. Research described here helps explain the lack of major crossreactivity between northern and southern grasses.PubMedCrossRefGoogle Scholar
  21. 21.
    Tinghino R, Twardosz A, Barletta B, et al.: Molecular, structural, and immunologic relationships between different families of recombinant calcium-binding pollen allergens. J Allergy Clin Immunol 2002, 109:314–320.PubMedCrossRefGoogle Scholar
  22. 22.
    Smith PM, Xu H, Swoboda I, Singh MB: Identification of a Ca2+ binding protein as a new Bermuda grass pollen allergen Cyn d 7: IgE cross-reactivity with oilseed rape allergen Bra r 1. Int Arch Allergy Immunol 1997, 114:265–271.PubMedCrossRefGoogle Scholar
  23. 23.
    van Ree R, Hoffman DR, van Dijk W, et al.: Lol p XI, a new major grass pollen allergen, is a member of a family of soybean trypsin inhibitor-related proteins. J Allergy Clin Immunol 1995, 95:970–978.PubMedCrossRefGoogle Scholar
  24. 24.
    Asturias JA, Arilla MC, Gomez-Bayon N, et al.: Cloning and high level expression of Cynodon dactylon (Bermuda grass) pollen profilin (Cyn d 12) in Escherichia coli: purification and characterization of the allergen. Clin Exp Allergy 1997, 27:1307–1313.PubMedCrossRefGoogle Scholar
  25. 25.
    Niederberger V, Laffer S, Froschl R, et al.: IgE antibodies to recombinant pollen allergens (Phl p 1, Phl p 2, Phl p 5, and Bet v 2) account for a high percentage of grass pollen-specific IgE. J Allergy Clin Immunol 1998, 101:258–264.PubMedCrossRefGoogle Scholar
  26. 26.
    Wurtzen PA, Nelson HS, Løwenstein H, Ipsen H: Characterization of Chenopodiales (Amaranthus retroflexus, Chenopodium album, Kochia scoparia, Salsola pestifer) pollen allergens. Allergy 1995, 50:489–497.PubMedCrossRefGoogle Scholar
  27. 27.
    Barderas R, Villalba M, Lombardero M, Rodriguez R: Identification and characterization of Che a 1 allergen from Chenopodium album pollen. Int Arch Allergy Immunol 2002, 127:47–54.PubMedCrossRefGoogle Scholar
  28. 28.
    Kernerman SM, McCullough J, Green J, Ownby DR: Evidence of cross-reactivity between olive, ash, privet, and Russian olive tree pollen allergens. Ann Allergy 1992, 69:493–496.PubMedGoogle Scholar
  29. 29.
    Bousquet J, Hewitt B, Guerin B, et al.: Allergy in the Mediterranean area. II: Cross-allergenicity among Urticaceae pollens (Parietaria and Urtica). Clin Allergy 1986, 16:57–64.PubMedCrossRefGoogle Scholar
  30. 30.
    Miura N: Ramie (Boehmeria nivea) pollen-induced bronchial asthma and allergenic cross-reactivity of ramie and Parietaria. Arerugi 1993, 42:649–655.PubMedGoogle Scholar
  31. 31.
    Stumvoll S, Westritschnig K, Lidholm J, et al.: Identification of cross-reactive and genuine Parietaria judaica pollen allergens. J Allergy Clin Immunol 2003, 111:974–749.PubMedCrossRefGoogle Scholar
  32. 32.
    Asero R, Mistrello G, Roncarolo D, Amato S: Parietaria profilin shows only limited cross-reactivity with birch and grass profilins. Int Arch Allergy Immunol 2003, 133:121–124.CrossRefGoogle Scholar
  33. 33.
    di Somma C, Fiore L, Di Lonardo A, et al.: Cross-reactivity between the major Parietaria allergen and rotovirus VP4 protein. Allergy 2003, 58:503–510. An interesting study reporting the first evidence of cross-reactivity between a pollen allergen and a viral antigen.CrossRefGoogle Scholar
  34. 34.
    Vallverdú A, Asturias JA, Arilla C, et al.: Characterization of recombinant Mercurialis annua major allergen Mer a 1 (profilin). J Allergy Clin Immunol 1998, 101:363–370.PubMedCrossRefGoogle Scholar
  35. 35.
    Vallier P, Ballard S, Harf R, et al.: Identification of profilin as an IgE-binding component in latex from Hevea brasiliensis: clinical implications. Clin Exp Allergy 1995, 25:332–339.PubMedCrossRefGoogle Scholar
  36. 36.
    Fuchs T, Spitzauer S, Vente C, et al.: Natural latex, grass pollen, and weed pollen share IgE epitopes. J Allergy Clin Immunol 1997, 100:356–364.PubMedCrossRefGoogle Scholar
  37. 37.
    Valenta R, Breiteneder H, Pettenberger K, et al.: Homology of the major birch-pollen allergen, Bet v I, with the major pollen allergens of alder, hazel, and hornbeam at the nucleic acid level as determined by cross-hybridization. J Allergy Clin Immunol 1991, 87:677–682.PubMedCrossRefGoogle Scholar
  38. 38.
    Niederberger V, Pauli G, Gronlund H, et al.: Recombinant birch pollen allergens (rBet v 1 and rBet v 2) contain most of the IgE epitopes present in birch, alder, hornbeam, hazel, and oak pollen: a quantitative IgE inhibition study with sera from different populations. J Allergy Clin Immunol 1998, 102:579–591.PubMedCrossRefGoogle Scholar
  39. 39.
    Bauer L, Ebner C, Hirschwehr R, et al.: IgE cross-reactivity between birch pollen, mugwort pollen and celery is due to at least three distinct cross-reacting allergens: immunoblot investigation of the birch-mugwort-celery syndrome. Clin Exp Allergy 1996, 26:1161–1170.PubMedCrossRefGoogle Scholar
  40. 40.
    Seiberler S, Scheiner O, Kraft D, et al.: Characterization of a birch pollen allergen, Bet v III, representing a novel class of Ca2+ binding proteins: specific expression in mature pollen and dependence of patients’ IgE binding on proteinbound Ca2+. EMBO J 1994, 13:3481–3486.PubMedGoogle Scholar
  41. 41.
    Engel E, Richter K, Obermeyer G, et al.: Immunological and biological properties of Bet v 4, a novel birch pollen allergen with two EF-hand calcium-binding domains. J Biol Chem 1997, 272:28630–28637.PubMedCrossRefGoogle Scholar
  42. 42.
    Karamloo F, Schmitz N, Scheuer S, et al.: Molecular cloning and characterization of a birch pollen minor allergen, Bet v 5, belonging to a family of isoflavone reductaserelated proteins. J Allergy Clin Immunol 1999, 104:991–999.PubMedCrossRefGoogle Scholar
  43. 43.
    Focke M, Hemmer W, Hayek B, et al.: Identification of allergens in oilseed rape (Brassica napus) pollen. Int Arch Allergy Immunol 1998, 117:105–112.PubMedCrossRefGoogle Scholar
  44. 44.
    Hayek B, Vangelista L, Pastore A, et al.: Molecular and immunologic characterization of a highly cross-reactive two EF-hand calcium-binding alder pollen allergen, Aln g 4: structural basis for calcium-modulated IgE recognition. J Immunol 1998, 161:7031–7039.PubMedGoogle Scholar
  45. 45.
    Neudecker P, Nerkamp J, Eisenmann A, et al.: Solution structure, dynamics, and hydrodynamics of the calcium-bound cross-reactive birch pollen allergen Bet v 4 reveal a canonical monomeric two EF-hand assembly with a regulatory function. J Mol Biol 2004, 336:1141–1157.PubMedCrossRefGoogle Scholar
  46. 46.
    Gruehn S, Suphioglu C, O’Hehir R, Volkmann D: Molecular cloning and characterization of hazel pollen protein (70kD) as a luminal binding protein (BiP): a novel cross-reactive plant allergen. Int Arch Allergy Immunol 2003, 131:91–100.PubMedCrossRefGoogle Scholar
  47. 47.
    Mittag D, Vieths S, Vogel L, et al.: Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. J Allergy Clin Immunol 2004, 113:148–154.PubMedCrossRefGoogle Scholar
  48. 48.
    Welch J, Jones MG, Cullinan P, et al.: Sensitization to oilseed rape is not due to cross-reactivity with grass pollen. Clin Exp Allergy 2000, 30:370–375.PubMedCrossRefGoogle Scholar
  49. 49.
    Calabozo B, Barber D, Polo F: Studies on the carbohydrate moiety of Pla l 1 allergen: identification of a major N-glycan and significance for the immunoglobulin E-binding activity. Clin Exp Allergy 2002, 32:1628–1634.PubMedCrossRefGoogle Scholar
  50. 50.
    Bousquet J, Guérin B, Hewitt B, et al.: Allergy in the Mediterranean area III. Cross reactivity among Oleaceae pollens. Clin Allergy 1985, 15:439–448.PubMedCrossRefGoogle Scholar
  51. 51.
    Obispo TM, Melero JA, Carpizo JA, et al.: The main allergen of Olea europaea (Ole e I) is also present in other species of the Oleaceae family. Clin Exp Allergy 1993, 23:311–316.PubMedCrossRefGoogle Scholar
  52. 52.
    Martin-Orozco E, Cárdaba B, del Pozo V, et al.: Ole e 1: epitope mapping, cross-reactivity with other Oleaceae pollens and ultrastructural localization. Int Arch Allergy Immunol 1994, 104:160–170.PubMedCrossRefGoogle Scholar
  53. 53.
    Batanero E, Villalba M, Monsalve R, Rodriguez R: Crossreactivity between the major allergen from olive pollen and unrelated glycoproteins: evidence of an epitope in the glycan moiety of the allergen. J Allergy Clin Immunol 1996, 97:1264–1271.PubMedCrossRefGoogle Scholar
  54. 54.
    Batanero E, Villalba M, Ledesma A, et al.: Ole e 3, an olive-tree allergen, belongs to a widespread family of pollen proteins. Eur J Biochem 1996, 241:772–778.PubMedCrossRefGoogle Scholar
  55. 55.
    Ledesma A, González E, Pascual CY, et al.: Are Ca2+-binding motifs involved in the immunoglobulin E-binding of allergens? Olive pollen allergens as model of study. Clin Exp Allergy 2002, 32:1476–1483.PubMedCrossRefGoogle Scholar
  56. 56.
    Barral P, Batanero E, Palomares O, et al.: A major allergen from pollen defines a novel family of plant proteins and shows intra- and interspecies cross-reactivity. J Immunol 2004, 172:3644–3651.PubMedGoogle Scholar
  57. 57.
    Niederberger V, Purohit A, Oster JP, et al.: The allergen profile of ash (Fraxinus excelsior) pollen: cross-reactivity with allergens from various plant species. Clin Exp Allergy 2002, 32:933–941.PubMedCrossRefGoogle Scholar
  58. 58.
    Förster-Waldi E, Marchetti M, Schℓl I, et al.: Type I allergy to elderberry (Sambucus nigra) is elicited by a 33.2 kDa allergen with significant homology to ribosomal inactivating proteins. Clin Exp Allergy 2003, 33:1703–1710.CrossRefGoogle Scholar
  59. 59.
    Rafnar T, Griffith IJ, Kuo M-C, et al.: Cloning of Amb a I (Antigen E), the major allergen family of short ragweed pollen. J Biol Chem 1991, 266:1229–1236.PubMedGoogle Scholar
  60. 60.
    Roebber M, Klapper DG, Marsh DG: Two isoallergens of short ragweed component Ra5. J Immunol 1982, 129:120–125.PubMedGoogle Scholar
  61. 61.
    Bond JF, Garman RD, Keating KM, et al.: Multiple Amb a I allergens demonstrate specific reactivity with IgE and T cells from ragweed-allergic patients. J Immunol 1991, 146:3380–3385.PubMedGoogle Scholar
  62. 62.
    Roebber M, Hussain R, Klapper DG, Marsh DG: Isolation and properties of a new short ragweed pollen allergen, Ra6. J Immunol 1983, 131:706–711.PubMedGoogle Scholar
  63. 63.
    Yunginger JW, Gleich GJ: Mesurement of ragweed antigen E by double antibody radioimmunoassay. J Allergy Clin Immunol 1972, 50:326–337.PubMedCrossRefGoogle Scholar
  64. 64.
    Lee YS, Dickinson DB: Characterization of pollen antigens from Ambrosia L. (Compositae) and related taxa by immunoelectrophoresis and radial immunodiffusion. Am J Bot 1979, 66:245–262.CrossRefGoogle Scholar
  65. 65.
    Krilis S, Baldo BA, Raison RL, et al.: Standardization of antigen E in ragweed pollen extracts using a monoclonal antibodybased enzyme immunoassay. J Allergy Clin Immunol 1983, 71:261–265.PubMedCrossRefGoogle Scholar
  66. 66.
    Coulter KM, Yang WH, Dorval G, et al.: Specific IgE antibody responses to ragweed allergens Ra5S and Ra5G associated with distinct HLA-DR b genes. Mol Immunol 1987, 24:1207–1210.PubMedCrossRefGoogle Scholar
  67. 67.
    Katial RK, Lin FL, Stafford WW, et al.: Mugwort and sage (Artemisia) pollen cross-reactivity: ELISA inhibition and immunoblot evaluation. Ann Allergy Asthma Immunol 1997, 79:340–346.PubMedCrossRefGoogle Scholar
  68. 68.
    Brandys J, Grimsøen A, Nilsen BM, et al.: Cross-reactivity between pollen extracts from six Artemisia species. Planta Med 1993, 59:221–228.PubMedCrossRefGoogle Scholar
  69. 69.
    Hirschwehr R, Heppner C, Spitzauer S, et al.: Identification of common allergenic structures in mugwort and ragweed pollen. J Allergy Clin Immunol 1998, 101:196–206.PubMedCrossRefGoogle Scholar
  70. 70.
    Wopfner N, Willeroidee M, Hebenstreit D, et al.: Molecular and immunological characterization of profilin from mugwort pollen. Biol Chem 2002, 383:1779–1789.PubMedCrossRefGoogle Scholar
  71. 71.
    Garcia-Sells FJ, Diaz-Perales A, Snchez-Monge R, et al.:Patterns of reactivity to lipid transfer proteins of plant foods and Artemisia pollen: an in vivo study. Int Arch Allergy Immunol 2002, 128:115–122.CrossRefGoogle Scholar
  72. 72.
    Fernandez C, Martin-Esteban M, Fiandor A, et al.: Analysis of cross-reactivity between sunflower pollen and other pollens of the Composite family. J Allergy Clin Immunol 1993, 92:660–667.PubMedCrossRefGoogle Scholar
  73. 73.
    Asturias JA, Arilla MC, Gomez-Bayon N, et al.: Cloning and immunological characterization of the allergen Hel a 2 (profilin) from sunflower pollen. Mol Immunol 1998, 35:469–478.PubMedCrossRefGoogle Scholar

Copyright information

© Current Science Inc 2004

Authors and Affiliations

  • Richard W. Weber
    • 1
  1. 1.National Jewish Medical and Research CenterDenverUSA

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