Allergens are defined as environmental agents that induce IgE-mediated immediate hypersensitivity reactions following inhalation, ingestion or injection. In some texts, allergens are described as ‘innocuous’ or‘harmless’, which is certainly true for the majority of non-sensitized individuals. However, for patients with hay fever, asthma or atopic dermatitis (AD), the majority of whom are sensitized to pollen or indoor allergens, exposure to allergens is far from harmless. Equally, local and systemic anaphylactic reactions to insect venom or food allergens are serious, and potentially life-threatening, problems for allergic patients. Little is understood about why certain allergens are associated with specific allergic conditions: why pollens cause hay fever, why asthma is strongly associated with indoor allergens and why peanut is such a potent cause of anaphylaxis. From the immunological point of view, it is important to distinguish between complete (‘true’, sensitising) allergens and incomplete (non-sensitising) allergens. Non-sensitising allergens are able to interact with IgE antibodies (which may or may not result in allergic symptoms), but are unable to induce the production of IgE antibodies. Their role as allergens fully depends on their cross-reactivity with complete (or sensitising) allergens. A good example of a non-sensitizing would be the apple allergen, Mal d 1, which is strongly cross-reactive with birch pollen, Bet v 1, but does not itself cause sensitization. While non-sensitizing cross-reacting allergens are of interest both from the clinical as well as from the immunological point of view, we focus in this chapter on allergenicity, the process that results in allergen-specific IgE synthesis.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Platts-Mills TA, Vervloet D, Thomas WR, Aalberse RC, Chapman MD (1997) Indoor allergens and asthma: report of the Third International Workshop. J Allergy Clin Immunol. 100:S2–24
Scheiner O, Breiteneder H, Dolocek C, Duchene M, Ebner C, Ferreira F, Hoffmann K, Schenk S, Valenta R, Kraft D (1994) Molecular and functional characterization of allergens: basic and practical aspects. Arb Paul Ehrlich Inst Bundesamt Sera Impfstoffe Frankf A M 221–232
Aalberse RC (2000) Structural biology of allergens. J Allergy Clin Immunol. 106:228–238
Aalberse RC, Stapel SO (2001) Structure of food allergens in relation to allergenicity. Pediatr Allergy Immunol. 12(Suppl 14):10–14
Chapman MD, Smith AM, Vailes LD, Arruda LK, Dhanaraj V, Pomés A (2000) Recombinant allergens for diagnosis and therapy of allergic disease. J Allergy Clin Immunol. 106:409–418
Wopfner N, Gadermaier G, Egger M, Asero R, Ebner C, Jahn-Schmid B, Ferreira F (2005) The spectrum of allergens in ragweed and mugwort pollen. Int Arch Allergy Immunol. 138:337–346
Chapman MD, Pomes A, Breiteneder H, Ferreira F (2007) Nomenclature and structural biology of allergens. J Allergy Clin Immunol. 119:414–420
Ferreira F, Wallner M, Thalhamer J (2004) Customized antigens for desensitizing allergic patients. Adv Immunol. 84:79–129
Thomas WR, Hales BJ, Smith WA (2005) Genetically engineered vaccines. Curr Allergy Asthma Rep. 5:197–203
Valenta R, Niederberger V (2007) Recombinant allergens for immunotherapy. J Allergy Clin Immunol. 119:826–830
Larche M, Akdis CA, Valenta R (2006) Immunological mechanisms of allergen-specific immunotherapy. Nat Rev Immunol. 6:761–771
Jenkins JA, Griffiths-Jones S, Shewry PR, Breiteneder H, Mills EN (2005) Structural related-ness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis. J Allergy Clin Immunol. 115:163–170
Radauer C, Breiteneder H (2006) Pollen allergens are restricted to few protein families and show distinct patterns of species distribution. J Allergy Clin Immunol. 117:141–147
van Oort E, Lerouge P, de Heer PG, Seveno M, Coquet L, Modderman PW, Faye L, Aalberse RC, van RR (2004) Substitution of Pichia pastoris-derived recombinant proteins with man-nose containing O- and N-linked glycans decreases specificity of diagnostic tests. Int Arch Allergy Immunol. 135:187–195
Hewitt CR, Brown AP, Hart BJ, Pritchard DI (1995) A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: innate protection by antipro-teases. J Exp Med. 182:1537–1544
Shakib F, Gough L (2000) The proteolytic activity of Der p 1 selectively enhances IgE synthesis: a link between allergenicity and cysteine protease activity. Clin Exp Allergy. 30:751–752
Asokananthan N, Graham PT, Stewart DJ, Bakker AJ, Eidne KA, Thompson PJ, Stewart GA (2002) House dust mite allergens induce proinflammatory cytokines from respiratory epithelial cells: the cysteine protease allergen, Der p 1, activates protease-activated receptor (PAR)-2 and inactivates PAR-1. J Immunol. 169:4572–4578
Wan H, Winton HL, Soeller C, Taylor GW, Gruenert DC, Thompson PJ, Cannell MB, Stewart GA, Garrod DR, Robinson C (2001) The transmembrane protein occludin of epithelial tight junctions is a functional target for serine peptidases from faecal pellets of Dermatophagoides pteronyssinus. Clin Exp Allergy. 31:279–294
King C, Brennan S, Thompson PJ, Stewart GA (1998) Dust mite proteolytic allergens induce cytokine release from cultured airway epithelium. J Immunol. 161:3645–3651
Platts-Mills TA (2007) The role of indoor allergens in chronic allergic disease. J Allergy Clin Immunol. 119:297–302
Platts-Mills T, Vaughan J, Squillace S, Woodfolk J, Sporik R (2001) Sensitisation, asthma, and a modified Th2 response in children exposed to cat allergen: a population-based cross-sectional study. Lancet. 357:752–756
Ownby DR, Johnson CC, Peterson EL (2002) Exposure to dogs and cats in the first year of life and risk of allergic sensitization at 6 to 7 years of age. JAMA. 288:963–972
Wallner M, Gruber P, Radauer C, Maderegger B, Susani M, Hoffmann-Sommergruber K, Ferreira F (2004) Lab scale and medium scale production of recombinant allergens in Escherichia coli. Methods. 32:219–226
Ferreira F, Hirtenlehner K, Jilek A, Godnik-Cvar J, Breiteneder H, Grimm R, Hoffmann-Sommergruber K, Scheiner O, Kraft D, Breitenbach M, Rheinberger HJ, Ebner C (1996) 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 183:599–609
Thomas WR, Hales BJ, Smith WA (2004) Recombinant allergens for analysing T-cell responses. Methods. 32:255–264
Schmid-Grendelmeier P, Crameri R (2001) Recombinant allergens for skin testing. Int Arch Allergy Immunol. 125:96–111
Smith AM, Chapman MD (1996) Reduction in IgE binding to allergen variants generated by site-directed mutagenesis: contribution of disulfide bonds to the antigenic structure of the major house dust mite allergen Der p 2. Mol Immunol. 33:399–405
Jutel M, Jaeger L, Suck R, Meyer H, Fiebig H, Cromwell O (2005) Allergen-specific immu-notherapy with recombinant grass pollen allergens. J Allergy Clin Immunol. 116:608–613
Rhyner C, Weichel M, Fluckiger S, Hemmann S, Kleber-Janke T, Crameri R (2004) Cloning allergens via phage display. Methods. 32:212–218
Chua KY, Doyle CR, Simpson RJ, Turner KJ, Stewart GA, Thomas WR (1990) Isolation of cDNA coding for the major mite allergen Der p II by IgE plaque immunoassay. Int Arch Allergy Appl Immunol. 91:118–123
Thomas WR, Stewart GA, Simpson RJ, Chua KY, Plozza TM, Dilworth RJ, Nisbet A, Turner KJ (1988) Cloning and expression of DNA coding for the major house dust mite allergen Der p 1 in Escherichia coli. Int Arch Allergy Appl Immunol. 85:127–129
Rafnar T, Griffith IJ, Kuo MC, Bond JF, Rogers BL, Klapper DG (1991) Cloning of Amb a I (antigen E), the major allergen family of short ragweed pollen. J Biol Chem. 266:1229–1236
Breiteneder H, Pettenburger K, Bito A, Valenta R, Kraft D, Rumpold H, Scheiner O, Breitenbach M (1989) The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene. EMBO J. 8:1935–1938
King TP, Hoffman D, Lowenstein H, Marsh DG, Platts-Mills TA, Thomas W (1994) Allergen nomenclature. WHO/IUIS Allergen Nomenclature Subcommittee. Int Arch Allergy Immunol. 105:224–233
Marsh DG, Goodfriend L, King TP, Lowenstein H, Platts-Mills TA (1986) Allergen nomenclature. Bull World Health Organ. 64:767–774
Piboonpocanun S, Malainual N, Jirapongsananuruk O, Vichyanond P, Thomas WR (2006) Genetic polymorphisms of major house dust mite allergens. Clin Exp Allergy. 36:510–516
Obermeyer G, Gehwolf R, Sebesta W, Hamilton N, Gadermaier G, Ferreira F, Commandeur U, Fischer R, Bentrup FW (2004) Over-expression and production of plant allergens by molecular farming strategies. Methods. 32:235–240
Vailes LD, Sun AW, Ichikawa K, Wu Z, Sulahian TH, Chapman MD, Guyre PM (2002) High-level expression of immunoreactive recombinant cat allergen (Fel d 1): targeting to antigen-presenting cells. J Allergy Clin Immunol. 110:757–762
Best EA, Stedman KE, Bozic CM, Hunter SW, Vailes L, Chapman MD, McCall CA, McDermott MJ (2000) A recombinant group 1 house dust mite allergen, rDer f 1, with biological activities similar to those of the native allergen. Protein Expr Purif. 20:462–471
Vailes LD, Kinter MT, Arruda LK, Chapman MD (1998) High-level expression of cockroach allergen, Bla g 4, in Pichia pastoris. J Allergy Clin Immunol. 101:274–280
van Ree R, van Leeuwen WA, Bulder I, Bond J, Aalberse RC (1999) Purified natural and recombinant Fel d 1 and cat albumin in in vitro diagnostics for cat allergy. J Allergy Clin Immunol. 104:1223–1230
Ball T, Edstrom W, Mauch L, Schmitt J, Leistler B, Fiebig H, Sperr WR, Hauswirth AW, Valent P, Kraft D, Almo SC, Valenta R (2005) Gain of structure and IgE epitopes by eukaryo-tic expression of the major Timothy grass pollen allergen, Phl p 1. FEBS J. 272:217–227
van Oort E, de Heer PG, van Leeuwen WA, Derksen NI, Muller M, Huveneers S, Aalberse RC, van RR (2002) Maturation of Pichia pastoris-derived recombinant pro-Der p 1 induced by deglycosylation and by the natural cysteine protease Der p 1 from house dust mite. Eur J Biochem. 269:671–679
Takai T, Kato T, Sakata Y, Yasueda H, Izuhara K, Okumura K, Ogawa H (2005) Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity but no serine protease activity. Biochem Biophys Res Commun. 328:944–952
Scheiner O, Kraft D (1995) Basic and practical aspects of recombinant allergens. Allergy. 50:384–391
Godnic-Cvar J, Susani M, Breiteneder H, Berger A, Havelec L, Waldhor T, Hirschwehr R, Valenta R, Scheiner O, Rudiger H, Kraft D, Ebner C (1997) Recombinant Bet v 1, the major birch pollen allergen, induces hypersensitivity reactions equal to those induced by natural Bet v 1 in the airways of patients allergic to tree pollen. J Allergy Clin Immunol. 99:354–359
Arruda LK, Vailes LD, Hayden ML, Benjamin DC, Chapman MD (1995) Cloning of cockroach allergen, Bla g 4, identifies ligand binding proteins (or calycins) as a cause of IgE antibody responses. J Biol Chem. 270:31196–31201
Pittner G, Vrtala S, Thomas WR, Weghofer M, Kundi M, Horak F, Kraft D, Valenta R (2004) Component-resolved diagnosis of house-dust mite allergy with purified natural and recom-binant mite allergens. Clin Exp Allergy. 34:597–603
Valenta R, Kraft D (2004) Recombinant allergens: from production and characterization to diagnosis, treatment, and prevention of allergy. Methods. 32:207–208
Erwin EA, Custis NJ, Satinover SM, Perzanowski MS, Woodfolk JA, Crane J, Wickens K, Platts-Mills TA (2005) Quantitative measurement of IgE antibodies to purified allergens using streptavidin linked to a high-capacity solid phase. J Allergy Clin Immunol. 115:1029–1035
Harwanegg C, Laffer S, Hiller R, Mueller MW, Kraft D, Spitzauer S, Valenta R (2003) Microarrayed recombinant allergens for diagnosis of allergy. Clin Exp Allergy. 33:7–13
King EM, Vailes, LD, Tsay A, Satinover SM, Chapman MD (2007) Simultaneous detection of total and allergen-specific IgE using purified allergens in a fluorescent multiplex array. J Allergy Clin Immunol. 120:1126–1131.
Smith WA, Chua KY, Kuo MC, Rogers BL, Thomas WR (1994) Cloning and sequencing of the Dermatophagoides pteronyssinus group III allergen, Der p III. Clin Exp Allergy. 24:220–228
Chua KY, Stewart GA, Thomas WR, Simpson RJ, Dilworth RJ, Plozza TM, Turner KJ (1988) Sequence analysis of cDNA coding for a major house dust mite allergen, Der p 1. Homology with cysteine proteases. J Exp Med. 167:175–182
Stewart GA, Robinson C (2003) The immunobiology of allergenic peptidases. Clin Exp Allergy. 33:3–6
Meno K, Thorsted PB, Ipsen H, Kristensen O, Larsen JN, Spangfort MD, Gajhede M, Lund K (2005) The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen. J Immunol. 175:3835–3845
de Halleux S., Stura E, VanderElst L, Carlier V, Jacquemin M, Saint-Remy JM (2006) Three-dimensional structure and IgE-binding properties of mature fully active Der p 1, a clinically relevant major allergen. J Allergy Clin Immunol. 117:571–576
Mahler V, Gutgesell C, Valenta R, Fuchs T (2006) Natural rubber latex and hymenoptera venoms share ImmunoglobinE-epitopes accounting for cross-reactive carbohydrate determinants. Clin Exp Allergy. 36:1446–1456
Takai T, Kato T, Yasueda H, Okumura K, Ogawa H (2005) Analysis of the structure and allergenicity of recombinant pro- and mature Der p 1 and Der f 1: major conformational IgE epitopes blocked by prodomains. J Allergy Clin Immunol. 115:555–563
Arruda LK, Vailes LD, Ferriani VP, Santos AB, Pomés A, Chapman MD (2001) Cockroach allergens and asthma. J Allergy Clin Immunol. 107:419–428
Radauer C, Willerroider M, Fuchs H, Hoffmann-Sommergruber K, Thalhamer J, Ferreira F, Scheiner O, Breiteneder H (2006) Cross-reactive and species-specific immunoglobulin E epitopes of plant profilins: an experimental and structure-based analysis. Clin Exp Allergy. 36:920–929
Gadermaier G, Dedic A, Obermeyer G, Frank S, Himly M, Ferreira F (2004) Biology of weed pollen allergens. Curr Allergy Asthma Rep. 4:391–400
Breiteneder H, Radauer C (2004) A classification of plant food allergens. J Allergy Clin Immunol. 113:821–830
Reese G, Schicktanz S, Lauer I, Randow S, Luttkopf D, Vogel L, Lehrer SB, Vieths S (2006) Structural, immunological and functional properties of natural recombinant Pen a 1, the major allergen of Brown Shrimp, Penaeus aztecus. Clin Exp Allergy. 36:517–524
Vieths S, Scheurer S, Ballmer-Weber B (2002) Current understanding of cross-reactivity of food allergens and pollen. Ann N Y Acad Sci. 964:47–68
Henriksen A, King TP, Mirza O, Monsalve RI, Meno K, Ipsen H, Larsen JN, Gajhede M, Spangfort MD (2001) Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily. Proteins. 45:438–448
King TP, Spangfort MD (2000) Structure and biology of stinging insect venom allergens. Int Arch Allergy Immunol. 123:99–106
Hurst JL, Payne CE, Nevison CM, Marie AD, Humphries RE, Robertson DH, Cavaggioni A, Beynon RJ (2001) Individual recognition in mice mediated by major urinary proteins. Nature. 414:631–634
Fan Y, Gore JC, Redding KO, Vailes LD, Chapman MD, Schal C (2005) Tissue localization and regulation by juvenile hormone of human allergen Bla g 4 from the German cockroach, Blattella germanica (L). Insect Mol Biol. 14:45–53
Gore JC, Schal C (2007) Cockroach allergen biology and mitigation in the indoor environment. Annu Rev Entomol. 52:439–463
Markovic-Housley Z, Degano M, Lamba D, von Roepenack-Lahaye E, Clemens S, Susani M, Ferreira F, Scheiner O, Breiteneder H (2003) Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier. J Mol Biol. 325:123–133
van Ree R, Antonicelli L, Akkerdaas JH, Pajno GB, Barberio G, Corbetta L, Ferro G, Zambito M, Garritani MS, Aalberse RC, Bonifazi F (1996) Asthma after consumption of snails in house-dust-mite-allergic patients: a case of IgE cross-reactivity. Allergy. 51:387–393
van Ree R, Antonicelli L, Akkerdaas JH, Garritani MS, Aalberse RC, Bonifazi F (1996) Possible induction of food allergy during mite immunotherapy. Allergy. 51:108–113
De Maat-Bleeker F, van Dijk AG, Berrens L (1985) Allergy to egg yolk possibly induced by sensitization to bird serum antigens. Ann Allergy. 54:245–248
Quirce S, Maranon F, Umpierrez A, de las HM, Fernandez-Caldas E, Sastre J (2001) Chicken serum albumin (Gal d 5*) is a partially heat-labile inhalant and food allergen implicated in the bird-egg syndrome. Allergy. 56:754–762
Gough L, Schulz O, Sewell HF, Shakib F (1999) The cysteine protease activity of the major dust mite allergen Der p 1 selectively enhances the immunoglobulin E antibody response. J Exp Med. 190:1897–1902
Sharma S, Lackie PM, Holgate ST (2003) Uneasy breather: the implications of dust mite allergens. Clin Exp Allergy. 33:163–165
Machado DC, Horton D, Harrop R, Peachell PT, Helm BA (1996) Potential allergens stimulate the release of mediators of the allergic response from cells of mast cell lineage in the absence of sensitization with antigen-specific IgE. Eur J Immunol. 26:2972–2980
Miike S, Kita H (2003) Human eosinophils are activated by cysteine proteases and release inflammatory mediators. J Allergy Clin Immunol. 111:704–713
Reed CE, Kita H (2004) The role of protease activation of inflammation in allergic respiratory diseases. J Allergy Clin Immunol. 114:997–1008
Kikuchi Y, Takai T, Kuhara T, Ota M, Kato T, Hatanaka H, Ichikawa S, Tokura T, Akiba H, Mitsuishi K, Ikeda S, Okumura K, Ogawa H (2006) Crucial commitment of proteolytic activity of a purified recombinant major house dust mite allergen Der p1 to sensitization toward IgE and IgG responses. J Immunol. 177:1609–1617
Sears MR, Greene JM, Willan AR, Wiecek EM, Taylor DR, Flannery EM, Cowan JO, Herbison GP, Silva PA, Poulton R (2003) A longitudinal, population-based, cohort study of childhood asthma followed to adulthood. N Engl J Med. 349:1414–1422
Arruda LK, Ferriani VP, Vailes LD, Pomés A, Chapman MD (2001) Cockroach allergens: environmental distribution and relationship to disease. Curr Allergy Asthma Rep. 1:466–473
Rosenstreich DL, Eggleston P, Kattan M, Baker D, Slavin RG, Gergen P, Mitchell H, Niff-Mortimer K, Lynn H, Ownby D, Malveaux F (1997) The role of cockroach allergy and exposure to cockroach allergen in causing morbidity among inner-city children with asthma. N Engl J Med. 336:1356–1363
Morgan WJ, Crain EF, Gruchalla RS, O'Connor GT, Kattan M, Evans R, III, Stout J, Malindzak G, Smartt E, Plaut M, Walter M, Vaughn B, Mitchell H (2004) Results of a home-based environmental intervention among urban children with asthma. N Engl J Med 351:1068–1080
Pomés A, Chapman MD, Vailes LD, Blundell TL, Dhanaraj V (2002) Cockroach allergen Bla g 2: structure, function, and implications for allergic sensitization. Am J Respir Crit Care Med 165:391–397
Wünschmann S, Gustchina A, Chapman MD, Pomés A (2005) Cockroach allergen Bla g 2: an unusual aspartic proteinase. J Allergy Clin Immunol 116:140–145
Gustchina A, Li M, Wünschmann S, Chapman MD, Pomés A, Wlodawer A (2005) Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition. J Mol Biol 348:433–444
Gruber A, Mancek M, Wagner H, Kirschning CJ, Jerala R (2004) Structural model of MD-2 and functional role of its basic amino acid clusters involved in cellular lipopolysaccharide recognition. J Biol Chem 279:28475–28482
Keber MM, Gradisar H, Jerala R (2005) MD-2 and Der p 2 - a tale of two cousins or distant relatives? J Endotoxin Res 11:186–192
Kaiser L, Gronlund H, Sandalova T, Ljunggren HG, van Hage-Hamsten M, Achour A, Schneider G (2003) The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family. J Biol Chem 278:37730–37735
Kaiser L, Velickovic TC, Badia-Martinez D, Adedoyin J, Thunberg S, Hallen D, Berndt K, Gronlund H, Gafvelin G, van HM, Achour A (2007) Structural Characterization of the Tetrameric form of the Major Cat Allergen Fel d 1. J Mol Biol 370:714–727
Eisenbarth SC, Piggott DA, Huleatt JW, Visintin I, Herrick CA, Bottomly K (2002) Lipopolysaccharide-enhanced, toll-like receptor 4-dependent T helper cell type 2 responses to inhaled antigen. J Exp Med 196:1645–1651
Woodfolk JA (2007) T-cell responses to allergens. J Allergy Clin Immunol 119:280–294
Hayashi T, Raz E (2006) TLR9-based immunotherapy for allergic disease. Am J Med 119:897–896
Virtanen T, Zeiler T, Mantyjarvi R (1999) Important animal allergens are lipocalin proteins: why are they allergenic? Int Arch Allergy Immunol 120:247–258
Paine K, Flower DR (2000) The lipocalin website. Biochim Biophys Acta 1482:351–352
Flower DR, North AC, Sansom CE (2000) The lipocalin protein family: structural and sequence overview. Biochim Biophys Acta 1482:9–24
Mitchell EB, Crow J, Chapman MD, Jouhal SS, Pope FM, Platts-Mills TA (1982) Basophils in allergen-induced patch test sites in atopic dermatitis. Lancet 1:127–130
Ardern-Jones MR, Black AP, Bateman EA, Ogg GS (2007) Bacterial superantigen facilitates epithelial presentation of allergen to T helper 2 cells. Proc Natl Acad Sci U S A 104:5557–5562
Aalberse RC (1996) Atopy and the ectopic immune response. Immunol Cell Biol 74:201–205
Durham SR, Smurthwaite L, Gould HJ (2000) Local IgE production. Am J Rhinol 14:305–307
Pawankar R (2001) Mast cells as orchestrators of the allergic reaction: the IgE-IgE receptor mast cell network. Curr Opin Allergy Clin Immunol 1:3–6
Gould HJ, Sutton BJ, Beavil AJ, Beavil RL, McCloskey N, Coker HA, Fear D, Smurthwaite L (2003) The biology of IgE and the basis of allergic disease. Annu Rev Immunol 21:579–628
Ryzhov S, Goldstein AE, Matafonov A, Zeng D, Biaggioni I, Feoktistov I (2004) Adenosine-activated mast cells induce IgE synthesis by B lymphocytes: an A2B-mediated process involving Th2 cytokines IL-4 and IL-13 with implications for asthma. J Immunol 172:7726–7733
Matzinger P (2002) The danger model: a renewed sense of self. Science 296:301–305
Brinkmann V, Heusser CH (1993) T cell-dependent differentiation of human B cells into IgM, IgG, IgA, or IgE plasma cells: high rate of antibody production by IgE plasma cells, but limited clonal expansion of IgE precursors. Cell Immunol 152:323–332
Le GG, Schultze N, Walti S, Einsle K, Finkelman F, Kosco-Vilbois MH, Heusser C (1996) The development of IgE + memory B cells following primary IgE immune responses. Eur J Immunol 26:3042–3047
Horst A, Hunzelmann N, Arce S, Herber M, Manz RA, Radbruch A, Nischt R, Schmitz J, Assenmacher M (2002) Detection and characterization of plasma cells in peripheral blood: correlation of IgE + plasma cell frequency with IgE serum titre. Clin Exp Immunol 130:370–378
Karnowski A, chatz-Straussberger G, Klockenbusch C, Achatz G, Lamers MC (2006) Inefficient processing of mRNA for the membrane form of IgE is a genetic mechanism to limit recruitment of IgE-secreting cells. Eur J Immunol 36:1917–1925
Arps V, Sudowe S, Kolsch E (1998) Antigen dose-dependent differences in IgE antibody production are not due to polarization towards Th1 and Th2 cell subsets. Eur J Immunol 28:681–686
Erwin EA, Ronmark E, Wickens K, Perzanowski MS, Barry D, Lundback B, Crane J, Platts-Mills TA (2007) Contribution of dust mite and cat specific IgE to total IgE: Relevance to asthma prevalence. J Allergy Clin Immunol 119:359–365
Aalberse RC, Platts-Mills TA (2004) How do we avoid developing allergy: modifications of the TH2 response from a B-cell perspective. J Allergy Clin Immunol 113:983–986
Platts-Mills TA (1979) Local production of IgG, IgA and IgE antibodies in grass pollen hay fever. J Immunol 122:2218–2225
Chapman MD, Platts-Mills TA, Gabriel M, Ng HK, Allan WG, Hill LE, Nunn AJ (1980) Antibody response following prolonged hyposensitization with Dermatophagoides pteronys-sinus extract. Int Arch Allergy Appl Immunol 61:431–440
Sudowe S, Rademaekers A, Kolsch E (1997) Antigen dose-dependent predominance of either direct or sequential switch in IgE antibody responses. Immunology 91:464–472
Cameron L, Gounni AS, Frenkiel S, Lavigne F, Vercelli D, Hamid Q (2003) S epsilon S mu and S epsilon S gamma switch circles in human nasal mucosa following ex vivo allergen challenge: evidence for direct as well as sequential class switch recombination. J Immunol 171:3816–3822
MacLennan IC, Toellner KM, Cunningham AF, Serre K, Sze DM, Zuniga E, Cook MC, Vinuesa CG (2003) Extrafollicular antibody responses. Immunol Rev 194:8–18
Norman PS, Winkenwerder WL, Lichtenstein LM (1968) Immunotherapy of hay fever with ragweed antigen E: comparisons with whole pollen extract and placebos. J Allergy 42:93–108
Gleich GJ, Jacob GL (1975) Immunoglobulin E antibodies to pollen allergens account for high percentages of total immunoglobulin E protein. Science 190:1106–1108
Creticos PS, Schroeder JT, Hamilton RG, Balcer-Whaley SL, Khattignavong AP, Lindblad R, Li H, Coffman R, Seyfert V, Eiden JJ, Broide D (2006) Immunotherapy with a ragweed-toll-like receptor 9 agonist vaccine for allergic rhinitis. N Engl J Med 355:1445–1455
Palmer K, Burks W (2006) Current developments in peanut allergy. Curr Opin Allergy Clin Immunol 6:202–206
van RR (2007) Indoor allergens: relevance of major allergen measurements and standardization. J Allergy Clin Immunol 119:270–277
Niederberger V, Horak F, Vrtala S, Spitzauer S, Krauth MT, Valent P, Reisinger J, Pelzmann M, Hayek B, Kronqvist M, Gafvelin G, Gronlund H, Purohit A, Suck R, Fiebig H, Cromwell O, Pauli G, van Hage-Hamsten M, Valenta R (2004) Vaccination with genetically engineered allergens prevents progression of allergic disease. Proc Natl Acad Sci U S A. 101(Suppl 2):14677–14682
Tighe H, Takabayashi K, Schwartz D, Van NG, Tuck S, Eiden JJ, Kagey-Sobotka A, Creticos PS, Lichtenstein LM, Spiegelberg HL, Raz E (2000) Conjugation of immunostimulatory DNA to the short ragweed allergen amb a 1 enhances its immunogenicity and reduces its allergenicity. J Allergy Clin Immunol 106:124–134
Zhu D, Kepley CL, Zhang K, Terada T, Yamada T, Saxon A (2005) A chimeric human-cat fusion protein blocks cat-induced allergy. Nat Med 11:446–449
Rhyner C, Kundig T, Akdis CA, Crameri R (2007) Targeting the MHC II presentation pathway in allergy vaccine development. Biochem Soc Trans 35:833–834
Yennawar NH, Li LC, Dudzinski DM, Tabuchi A, Cosgrove DJ (2006) Crystal structure and activities of EXPB1 (Zea m 1), a beta-expansin and group-1 pollen allergen from maize. Proc Natl Acad Sci U S A 103:14664–14671
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Springer
About this chapter
Cite this chapter
Chapman, M.D., Pomés, A., Aalberse, R.C. (2009). Molecular Biology of Allergens: Structure and Immune Recognition. In: Pawankar, R., Holgate, S.T., Rosenwasser, L.J. (eds) Allergy Frontiers: Epigenetics, Allergens and Risk Factors. Allergy Frontiers, vol 1. Springer, Tokyo. https://doi.org/10.1007/978-4-431-72802-3_16
Download citation
DOI: https://doi.org/10.1007/978-4-431-72802-3_16
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-72801-6
Online ISBN: 978-4-431-72802-3
eBook Packages: MedicineMedicine (R0)