Cross-reactivity of pollen allergens: Recommendations for immunotherapy vaccines

Current Opinion in Allergy and Clinical Immunology

Volumn 5, Issue 6, 2005, Pages 563-569

  Weber, Richard W ^a,b  

^a NATIONAL JEWISH MEDICAL AND RESEARCH CENTER   (United States)

^b NONE   (United States)

Author keywords

Cross reactivity; Immunotherapy; Pollen allergen; Vaccine

Indexed keywords

CALCIUM BINDING PROTEIN; HEAT SHOCK PROTEIN 70; HERBACEOUS AGENT; IMMUNOGLOBULIN E; LIPID TRANSFER PROTEIN; POLLEN ANTIGEN; PROFILIN; RECOMBINANT DNA;

ACER; ALLERGENICITY; AMARANTHUS; ANGIOSPERM; ARTEMISIA; ARTICLE; ASTERACEAE; ATRIPLEX; BETULACEAE; BIRCH; CHENOPODIUM ALBUM; CONIFER; CROSS REACTION; DRUG DOSE REGIMEN; DRUG FORMULATION; DRUG IDENTIFICATION; DRUG ISOLATION; ENZYME ACTIVITY; FRAXINUS; FRUIT; GYMNOSPERM; HUMAN; IMMUNOMODULATION; IMMUNOREACTIVITY; IMMUNOTHERAPY; JUNIPERUS; OAK; OLIVE TREE; PARIETARIA; PATHOGENESIS; PLANT TAXONOMY; POLLEN; POLLEN ALLERGY; PRIORITY JOURNAL; PROTEIN FAMILY; RAGWEED; SALSOLA; SIDE EFFECT; SUNFLOWER; TREE; WEED;

EID: 27944496015     PISSN: 15284050     EISSN: 14736322     Source Type: Journal    
DOI: 10.1097/01.all.0000191240.28255.ab     Document Type: Article

References (66)

1. Mothes N, Horak F, Valenta R. Transition from a botanical to a molecular classification in tree pollen allergy: implications for diagnosis and therapy. Int Arch Allergy Immunol 2004; 135:357-373. An important discussion of the value of characterized allergens as markers in diagnosis, and ultimately, treatment. Represents a paradigm shift away from classic plant systematics.
2. Weber RW. Patterns of pollen cross-allergenicity. J Allergy Clin Immunol 2003; 112:229-239.
3. Weber RW. Cross-reactivity of pollen allergens. Curr Allergy Asthma Rep 2004; 4:401-408. This is an up to date broader review of pollen allergens. There is a tabulation of grass pollen allergen groups and a cladogram of the grass family, clarifying relationships.
4. Gadermaier G, Dedic A, Obermeyer G, et al. Biology of weed pollen allergens. Curr Allergy Asthma Rep 2004; 4:391-400. Provides a very nice discussion of weed pollen allergens and a good up to date review. There is an excellent summary table delineating aspects of characterized weed allergens.
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.
6. 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.
7. 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.
8. van Ree R. Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases. Int Arch Allergy Immunol 2002; 129:189-197.
9. Ohtsuki T, Taniguchi Y, Kohno K, et al. Cry j 2, a major allergen of Japanese cedar pollen, shows polymethylgalacturonase activity. Allergy 1995; 50:90-93.
10. 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.
11. Andersson K, Lidholm J. Characteristics and immunobiology of grass pollen allergens. Int Arch Allergy Immunol 2003; 130:87-107.
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.
13. 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 Invest Allergol Clin Immunol 2002; 12:279-286.
14. 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.
15. Davies JM, Bright ML, Rolland JM, O'Hehir RE. Bahia grass pollen specific IgE is common in seasonal rhinitis patients but has limited cross-reactivity with ryegrass. Allergy 2005; 60:251-255. Little attention has been paid to Panicum grasses, and this paper offers an early insight into this group.
16. 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.
17. 2+ 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.
18. 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.
19. 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.
20. 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.
21. Asturias JA, Ibarrola I, Fernández J, et al. Pho d 2, a major allergen from date palm, is a profiling: cloning, sequencing, and immunoglobulin E cross-reactivity with other pollens. Clin Exp Allergy 2005; 35:374-381. An excellent characterization of a major allergen from a non-grass monocot - little work has been published in this arena.
22. 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.
23. Barderas R, Villalba M, Pascual CY, et al. Profilin (Che a 2) and polcalcin (Che a 3) are relevant allergens of Chenopodium album pollen: isolation, amino acid sequences, and immunologic properties. J Allergy Clin Immunol 2004; 113:1192-1198. Earlier work has suggested a high degree of cross-reactivity of lamb's quarter with other family members. This work may help explain the nature of that relationship.
24. Barderas R, Villalba M, Rodriguez R. Recombinant expression, purification and cross-reactivity of chenopod profilin: rChe a 2 as a good marker for profilin sensitization. Biol Chem 2004; 385:731-737. Profilins were described as the earliest panallergen, this report characterizes an important member of that group of allergens.
25. 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.
26. Sastre J, Lluch-Bernal M, Bustillo AMG, et al. Allergenicity and cross-reactivity of Russian olive pollen (Eleagnus angustifolia). Allergy 2004; 59:1181-1186. This report follows up on earlier work on a puzzling cross-reactivity.
27. Stumvoll S, Westritschnig K, Lidholm J, et al. Identification of cross-reactive and genuine Parietaria judaica pollen allergens. J Allergy Clin Immunol 2003; 111:974-979.
28. Sharma S, Panzani RC, Gaur SN, et al. Evaluation of cross-reactivity between Holoptelea integrifolia and Parietaria judaica. Int Arch Allergy Immunol 2005; 136:103-112. This is a recent report of relationships between botanically related but geographically disparate plants.
29. 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.
30. Asturias JA, Ibarrola I, Eseverri JL, et al. PCR-based cloning and immunological characterization of Parietaria judaica pollen profilin. J Investig Allergol Clin Immunol 2004; 14:43-48. Further work on allergens from a very important inducer of pollinosis.
31. 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.
32. 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.
33. 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.
34. 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.
35. 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.
36. 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. Another example of cross-reactivity between pollen and foods because of yet another shared allergen.
37. 142-156 is the dominant T-cell epitope of the major birch pollen allergen and important for cross-reactivity with Bet v 1-related food allergens. J Allergy Clin Immunol 2005; 116:213-219. The characterization of the dominant T-cell epitope on a very important and ubiquitous allergen. This work carries immense potential for tailoring vaccine immunotherapy in the future.
38. 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 protein-bound Ca2+. EMBO J 1994; 13:3481-3486.
39. 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.
40. 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 reductase-related proteins. J Allergy Clin Immunol 1999; 104:991-999.
41. 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.
42. 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.
43. 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.
44. 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. A well-performed work not only on the primary function of polcalcins, but an investigation of the similarities across botanical borders despite structural differences.
45. Gruehn S, Suphioglu C, O'Hehir R, Volkmann D. Molecular cloning and characterization of hazel pollen protein (70 kD) as a luminal binding protein (BiP): a novel cross-reactive plant allergen. Int Arch Allergy Immunol 2003; 131:91-100.
46. 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.
47. 2+-binding motifs involved in the immunoglobulin E-binding of allergens? Olive pollen allergens as model of study. Clin Exp Allergy 2002; 32:1476-1483.
48. Butteroni C, Afferni C, Barletta B, et al. Cloning and expression of the Olea europaea allergen Ole e 5, the pollen Cu/Zn superoxide dismutase. Int Arch Allergy Immunol 2005; 137:9-17. The first description of a copper/zinc superoxide dismutase as an allergen (manganese superoxide dismutase has been identified as an allergen). Although still considered a minor allergen, over a third of olive-sensitive patients related to this allergen.
49. 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. The description and characterization of yet another important olive pollen allergen, with far-reaching cross-reactivity potential.
50. 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.
51. Yunginger JW, Gleich GJ. Measurement of ragweed antigen E by double antibody radioimmunoassay. J Allergy Clin Immunol 1972; 50:326-337.
52. 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.
53. 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.
54. Brandys J, Grimsøen A, Nilsen BM, et al. Cross-reactivity between pollen extracts from six Artemisia species. Planta Med 1993; 59:221-228.
55. 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.
56. Himly M, Jahn-Schmid B, Dedic A, et al. Art v 1, the major allergen of mugwort pollen, is a modular glycoprotein with a defensin-like and a hydroxyproline-rich domain. FASEB J 2002; 17:106-108; E-pub: 15 November 2002.
57. Leonard R, Petersen BO, Himly M, et al. Two novel types of O-glycans on the mugwort pollen allergen Art v 1 and their role in antibody binding. J Biol Chem 2005; 9:7932-7940. The further characterization of some unique properties of a major mugwort allergen.
58. Lombardero M, Garcia-Sellés FJ, Polo F, et al. Prevalence of sensitization to Artemisia allergens Art v 1, Art v 3 and Art v 60 kDa. Cross-reactivity among Art v 3 and other relevant lipid-transfer protein allergens. Clin Exp Allergy 2004; 34:1415-1421. Well conducted research especially on the identification of Art v 3 as a nsLTP; again, a central actor in pollen-food cross-reactivity.
59. Garcia-Sellés FJ, Diaz-Perales A, Sánchez-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.
60. Salcedo G, Sanchez-Monge R, Diaz-Perales A, et al. Plant non-specific lipid transfer proteins as food and pollen allergens. Clin Exp Allergy 2004; 34:1336-1341. A useful review of an important class of ubiquitous panallergens, and the role of geographical differences.
61. Breiteneder H, Mills C. Nonspecific lipid-transfer proteins in plant foods and pollens: an important allergen class. Curr Opin Allergy Clin Immunol 2005; 5:275-279. An up to date discussion of the importance of this class of panallergens in both pollen and food sensitivity.
62. Wopfner N, Willeroidee M, Hebenstreit D, et al. Molecular and immunological characterization of profilin from mugwort pollen. Biol Chem 2002; 383:1779-1789.
63. 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.
64. 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.
65. Ibarrola I, Arilla MC, Martinez A, Asturias JA. Identification of a polygalacturonase as a major allergen (Pla a 2) from Platanus acerifolia pollen. J Allergy Clin Immunol 2004; 113:1185-1191. The investigation of a major allergen from an aeroallergen source that is recently receiving more attention. Characterization again shows the ubiquitous nature of some of these proteins in nature.
66. Enrique E, Alonso R, Bartolome B, et al. IgE reactivity to profilin in platanus acerifolia pollen-sensitized subjects with plant-derived food allergy. J Invest Allergol Clin Immunol 2004; 14:335-342.