Among other legal regulations, the Note for Guidance on Allergen Products CPMP/BWP/243/96 released by the European Medicines Agency provides regulatory instructions regarding the quality of allergen extracts for diagnostic or therapeutic purposes. The current revision of this guideline intends to transform the so-called ‘principle of taxonomic families’ to the ‘principle of homologous groups’. According to this concept, the data of one allergen extract demonstrating stability, efficacy and safety can, to a limited extent, be extrapolated to other allergen extracts belonging to the same homologous groups. The present work proposes the formation of homologous groups for pollen species and animal-derived materials on the basis of similar biochemical composition and homology/cross-reactivity of allergens or allergen sources. Some tree pollen species could be assigned to three different homologous groups, some weed pollen species to one homologous group and numerous grass pollen species to one homologous group on condition that data rely on single defined representative species. A homologous group for mites is limited to the Dermatophagoides species and the grouping of vertebrate-derived materials such as dander could be possible under restrictions. The criteria for the formation of the proposed homologous groups are illustrated in detail to provide an opportunity for extending existing homologous groups by further species in case of new insights in allergens and cross-reactivity of allergen sources. In this way, the concept of homologous groups could serve as a dynamic tool in the regulation of allergen products.

Monograph: Allergen Products – Producta allergenica; in European Directorate for the Quality of Medicines (EDQM) (ed): European Pharmacopoeia, ed 6. Strasbourg, Council of Europe, 2008, pp 679–680.
Committee for Proprietary Medicinal Products (CPMP) and Biotechnology Working Party (BWP): Note for Guidance on Allergen Products. 1996;CPMP/BWP/243/96.
Pini C: Summary of the regulators’ session. Arb Paul Ehrlich Inst Bundesamt Sera Impfstoffe Frankf AM 2006;95:45–48.
Committee for Medicinal Products for Human Use (CHMP) and Biologics Working Party (BWP): Concept Paper on the revision of the Note for Guidance on Allergen Products (CPMP/BWP/243/96): Production and quality issues. 2005; CHMP/BWP/229472/ 2005.
Allergome – A database of allergenic molecules.
International Union of Immunological Societies (IUIS) – Allergen Nomenclature Sub-Committee: The official ‘List of Allergens’. Update March 10, 2008.
The National Center for Biotechnology Information (NCBI) Taxonomy Database.
Larsen JN, Stroman P, Ipsen H: PCR based cloning and sequencing of isogenes encoding the tree pollen major allergen Car b I from Carpinus betulus, hornbeam. Mol Immunol 1992;29:703–711.
Tinghino R, Twardosz A, Barletta B, Puggioni EM, Iacovacci P, Butteroni C, Afferni C, Mari A, Hayek B, di Felice G, Focke M, Westritschnig K, Valenta R, Pini C: Molecular, structural, and immunologic relationships between different families of recombinant calcium-binding pollen allergens. J Allergy Clin Immunol 2002;109:314–320.
Niederberger V, Pauli G, Gronlund H, Froschl R, Rumpold H, Kraft D, Valenta R, Spitzauer S: 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.
Ipsen H, Hansen OC: The NH2-terminal amino acid sequence of the immunochemically partial identical major allergens of alder (Alnus glutinosa) Aln g I, birch (Betula verrucosa) Bet v I, hornbeam (Carpinus betulus) Car b I and oak (Quercus alba) Que a I pollens. Mol Immunol 1991;28:1279–1288.
Rohac M, Birkner T, Reimitzer I, Bohle B, Steiner R, Breitenbach M, Kraft D, Scheiner O, Gabl F, Rumpold H: The immunological relationship of epitopes on major tree pollen allergens. Mol Immunol 1991;28:897–906.
Valenta R, Breiteneder H, Petternburger K, Breitenbach M, Rumpold H, Kraft D, Scheiner O: 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.
Wiedemann P, Giehl K, Almo SC, Fedorov AA, Girvin M, Steinberger P, Rudiger M, Ortner M, Sippl M, Dolecek C, Kraft D, Jockusch B, Valenta R: Molecular and structural analysis of a continuous birch profilin epitope defined by a monoclonal antibody. J Biol Chem 1996;271:29915–29921.
Jung K, Schlenvoigt G, Jäger L: Allergologic[-]immunochemical study of tree and bush pollen. III. Cross reactions of human IgE antibodies with various tree pollen allergens (in German). Allerg Immunol (Leipz) 1987;33:223–230.
Engel E, Richter K, Obermeyer G, Briza P, Kungl AJ, Simon B, Auer M, Ebner C, Rheinberger HJ, Breitenbach M, Ferreira F: 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.
Verdino P, Barderas R, Villalba M, Westritschnig K, Valenta R, Rodriguez R, Keller W: Three-dimensional structure of the cross-reactive pollen allergen Che a 3: visualizing cross-reactivity on the molecular surfaces of weed, grass, and tree pollen allergens. J Immunol 2008;180:2313–2321.
Niederberger V, Hayek B, Vrtala S, Laffer S, Twardosz A, Vangelista L, Sperr WR, Valent P, Rumpold H, Kraft D, Ehrenberger K, Valenta R, Spitzauer S: Calcium-dependent immunoglobulin E recognition of the apo- and calcium-bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7. FASEB J 1999;13:843–856.
Twardosz A, Hayek B, Seiberler S, Vangelista L, Elfman L, Gronlund H, Kraft D, Valenta R: Molecular characterization, expression in Escherichia coli, and epitope analysis of a two EF-hand calcium-binding birch pollen allergen, Bet v 4. Biochem Biophys Res Commun 1997;239:197–204.
Neudecker P, Nerkamp J, Eisenmann A, Nourse A, Lauber T, Schweimer K, Lehmann K, Schwarzinger S, Ferreira F, Rosch P: 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.
Gruehn S, Suphioglu C, O’Hehir RE, 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.
Martin-Orozco E, Cardaba B, del Pozo V, de Andres B, Villalba M, Gallardo S, Rodriguez-Garcia MI, Fernandez MC, Alche JD, Rodriguez R: Ole e I: epitope mapping, cross-reactivity with other Oleaceaepollens and ultrastructural localization. Int Arch Allergy Immunol 1994;104:160–170.
Palomares O, Swoboda I, Villalba M, Balic N, Spitzauer S, Rodriguez R, Valenta R: The major allergen of olive pollen Ole e 1 is a diagnostic marker for sensitization to Oleaceae. Int Arch Allergy Immunol 2006;141:110–118.
Ledesma A, Villalba M, Batanero E, Rodriguez R: Molecular cloning and expression of active Ole e 3, a major allergen from olive-tree pollen and member of a novel family of Ca2+-binding proteins (polcalcins) involved in allergy. Eur J Biochem 1998;258:454–459.
Niederberger V, Purohit A, Oster JP, Spitzauer S, Valenta R, Pauli G: The allergen profile of ash (Fraxinus excelsior) pollen: cross-reactivity with allergens from various plant species. Clin Exp Allergy 2002;32:933–941.
Ledesma A, Barderas R, Westritschnig K, Quiralte J, Pascual CY, Valenta R, Villalba M, Rodriguez R: A comparative analysis of the cross-reactivity in the polcalcin family including Syr v 3, a new member from lilac pollen. Allergy 2006;61:477–484.
Duffort O, Palomares O, Lombardero M, Villalba M, Barber D, Rodriguez R, Polo F: Variability of Ole e 9 allergen in olive pollen extracts: relevance of minor allergens in immunotherapy treatments. Int Arch Allergy Immunol 2006;140:131–138.
Huecas S, Villalba M, Rodriguez R: Ole e 9, a major olive pollen allergen is a 1,3-beta-glucanase. Isolation, characterization, amino acid sequence, and tissue specificity. J Biol Chem 2001;276:27959–27966.
Palomares O, Villalba M, Quiralte J, Polo F, Rodriguez R: 1,3-β-glucanases as candidates in latex-pollen-vegetable food cross-reactivity. Clin Exp Allergy 2005;35:345–351.
Barral P, Batanero E, Palomares O, Quiralte J, Villalba M, Rodriguez R: 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.
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.
Bousquet J, Guerin B, Hewitt BE, Lim S, Michel FB: Allergy in the Mediterranean area. III: cross reactivity among Oleaceaepollens. Clin Allergy 1985;15:439–448.
Midoro-Horiuti T, Mathura V, Schein CH, Braun W, Yu S, Watanabe M, Lee JC, Brooks EG, Goldblum RM: Major linear IgE epitopes of mountain cedar pollen allergen Jun a 1 map to the pectate lyase catalytic site. Mol Immunol 2003;40:555–562.
Cortegano I, Civantos E, Aceituno E, del Moral A, Lopez E, Lombardero M, del Pozo V, Lahoz C: Cloning and expression of a major allergen from Cupressus arizonica pollen, Cup a 3, a PR-5 protein expressed under polluted environment. Allergy 2004;59:485–490.
GenBank – National Institutes of Health (NIH) genetic sequence database.
Swiss-Prot – Protein knowledgebase.
Tinghino R, Barletta B, Palumbo S, Afferni C, Iacovacci P, Mari A, di Felice G, Pini C: 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.
Mari A, Wallner M, Ferreira F: Fagales pollen sensitization in a birch-free area: a respiratory cohort survey using Fagalespollen extracts and birch recombinant allergens (rBet v 1, rBet v 2, rBet v 4). Clin Exp Allergy 2003;33:1419–1428.
Mur P, Feo Brito F, Lombardero M, Barber D, Galindo PA, Gomez E, Borja J: Allergy to linden pollen (Tilia cordata). Allergy 2001;56:457–458.
Asturias JA, Ibarrola I, Eraso E, Arilla MC, Martinez A: The major Platanus acerifolia pollen allergen Pla a 1 has sequence homology to invertase inhibitors. Clin Exp Allergy 2003;33:978–985.
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.
Andersson K, Lidholm J: Characteristics and immunobiology of grass pollen allergens. Int Arch Allergy Immunol 2003;130:87–107.
van Ree R, van Leeuwen WA, Aalberse RC: How far can we simplify in vitrodiagnostics for grass pollen allergy? A study with 17 whole pollen extracts and purified natural and recombinant major allergens. J Allergy Clin Immunol 1998;102:184–190.
van Ree R, Clemens JG, Aalbers M, Stapel SO, Aalberse RC: Characterization with monoclonal and polyclonal antibodies of a new major allergen from grass pollen in the group I molecular weight range. J Allergy Clin Immunol 1989;83:144–151.
Freidhoff LR, Ehrlich-Kautzky E, Grant JH, Meyers DA, Marsh DG: A study of the human immune response to Lolium perenne (rye) pollen and its components, Lol p I and Lol p II (rye I and rye II). I. Prevalence of reactivity to the allergens and correlations among skin test, IgE antibody, and IgG antibody data. J Allergy Clin Immunol 1986;78:1190–1201.
Stewart GA, Thompson PJ: The biochemistry of common aeroallergens. Clin Exp Allergy 1996;26:1020–1044.
Matthiesen F, Lowenstein H: Group V allergens in grass pollens. II. Investigation of group V allergens in pollens from 10 grasses. Clin Exp Allergy 1991;21:309–320.
Niederberger V, Laffer S, Froschl R, Kraft D, Rumpold H, Kapiotis S, Valenta R, Spitzauer S: 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.
Rossi RE, Monasterolo G, Monasterolo S: Measurement of IgE antibodies against purified grass-pollen allergens (Phl p 1, 2, 3, 4, 5, 6, 7, 11, and 12) in sera of patients allergic to grass pollen. Allergy 2001;56:1180–1185.
Esch RE, Klapper DG: Cross-reactive and unique grass group I antigenic determinants defined by monoclonal antibodies. J Allergy Clin Immunol 1987;79:489–495.
Laffer S, Valenta R, Vrtala S, Susani M, van Ree R, Kraft D, Scheiner O, Duchene M: Complementary DNA cloning of the major allergen Phl p I from timothy grass (Phleum pratense); recombinant Phl p I inhibits IgE binding to group I allergens from eight different grass species. J Allergy Clin Immunol 1994;94:689–698.
Leduc-Brodard V, Inacio F, Jaquinod M, Forest E, David B, Peltre G: Characterization of Dac g 4, a major basic allergen from Dactylis glomerata pollen. J Allergy Clin Immunol 1996;98:1065–1072.
Esch RE, Klapper DG: Identification and localization of allergenic determinants on grass group I antigens using monoclonal antibodies. J Immunol 1989;142:179–184.
Standring R, Spackman V, Porter SJ: Distribution of a major allergen of rye grass (Lolium perenne) pollen between other grass species. Int Arch Allergy Appl Immunol 1987;83:96–103.
van Ree R, Driessen MN, van Leeuwen WA, Stapel SO, Aalberse RC: Variability of crossreactivity of IgE antibodies to group I and V allergens in eight grass pollen species. Clin Exp Allergy 1992;22:611–617.
Leiferman KM, Gleich GJ: The cross-reactivity of IgE antibodies with pollen allergens. I. Analyses of various species of grass pollens. J Allergy Clin Immunol 1976;58:129–139.
Leiferman KM, Gleich GJ, Jones RT: The cross-reactivity of IgE antibodies with pollen allergens. II. Analyses of various species of ragweed and other fall weed pollens. J Allergy Clin Immunol 1976;58:140–148.
Martin BG, Mansfield LE, Nelson HS: Cross-allergenicity among the grasses. Ann Allergy 1985;54:99–104.
Esch RE, Klapper DG: Isolation and characterization of a major cross-reactive grass group I allergenic determinant. Mol Immunol 1989;26:557–561.
Smith PM, Ong EK, Knox RB, Singh MB: Immunological relationships among group I and group V allergens from grass pollen. Mol Immunol 1994;31:491–498.
Weber RW: Patterns of pollen cross-allergenicity. J Allergy Clin Immunol 2003;112:229–239.
Weber RW: Cross-reactivity of pollen allergens. Curr Allergy Asthma Rep 2004;4:401–408.
Mohapatra SS, Lockey RF, Shirley S: Immunobiology of grass pollen allergens. Curr Allergy Asthma Rep 2005;5:381–387.
Esch RE: Grass pollen allergens. Clin Allergy Immunol 2004;18:185–205.
Kahn CR, Marsh DG: Monoclonal antibodies to the major Lolium perenne (rye grass) pollen allergen Lol p I (Rye I). Mol Immunol 1986;23:1281–1288.
Arilla MC, Ibarrola I, Eraso E, Aguirre M, Martinez A, Asturias JA: Quantification in mass units of group 1 grass allergens by a monoclonal antibody-based sandwich ELISA. Clin Exp Allergy 2001;31:1271–1278.
Smith PM, Suphioglu C, Griffith IJ, Theriault K, Knox RB, Singh MB: Cloning and expression in yeast Pichia pastoris of a biologically active form of Cyn d 1, the major allergen of Bermuda grass pollen. J Allergy Clin Immunol 1996;98:331–343.
Matthiesen F, Schumacher MJ, Lowenstein H: Characterization of the major allergen of Cynodon dactylon (Bermuda grass) pollen, Cyn d I. J Allergy Clin Immunol 1991;88:763–774.
Han SH, Chang ZN, Chi CW, Perng HJ, Liu CC, Tsai JJ, Tam MF: Use of monoclonal antibodies to isolate and characterize Cyn d I, the major allergen of Bermuda grass pollen. J Allergy Clin Immunol 1993;92:549–558.
Duffort O, Quintana J, Ipsen H, Barber D, Polo F: Antigenic similarity among group 1 allergens from grasses and quantitation ELISA using monoclonal antibodies to Phl p 1. Int Arch Allergy Immunol 2008;145:283–290.
Suphioglu C, Ferreira F, Knox RB: Molecular cloning and immunological characterisation of Cyn d 7, a novel calcium-binding allergen from Bermuda grass pollen. FEBS Lett 1997;402:167–172.
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 pollen allergen Bra r 1. Int Arch Allergy Immunol 1997;114:265–271.
Hirschwehr R, Heppner C, Spitzauer S, Sperr WR, Valent P, Berger U, Horak F, Jäger S, Kraft D, Valenta R: Identification of common allergenic structures in mugwort and ragweed pollen. J Allergy Clin Immunol 1998;101:196–206.
Ayuso R, Carreira J, Lombardero M, Duffort O, Peris A, Basomba A, Polo F: Isolation by mAb based affinity chromatography of two Par j I isoallergens. Comparison of their physicochemical, immunochemical and allergenic properties. Mol Immunol 1993;30:1347–1354.
Stumvoll S, Westritschnig K, Lidholm J, Spitzauer S, Colombo P, Duro G, Kraft D, Geraci D, Valenta R: Identification of cross-reactive and genuine Parietaria judaica pollen allergens. J Allergy Clin Immunol 2003;111:974–979.
Asero R, Mistrello G, Roncarolo D, Casarini M: Detection of allergens in plantain (Plantago lanceolata) pollen. Allergy 2000;55:1059–1062.
Garcia Ortiz JC, Ventas P, Cosmes P, Lopez-Asunsolo A: An immunoblotting analysis of cross-reactivity between melon, and plantago and grass pollens. J Investig Allergol Clin Immunol 1996;6:378–382.
Calabozo B, Diaz-Perales A, Salcedo G, Barber D, Polo F: Cloning and expression of biologically active Plantago lanceolata pollen allergen Pla l 1 in the yeast Pichia pastoris. Biochem J 2003;372:889–896.
Hoffman DR, Miller JS, Sutton JL: Hymenoptera venom allergy: a geographic study. Ann Allergy 1980;45:276–279.
Mueller U, Roth A, Yman L, Patrizzi R: Use of RAST technique in wasp sting hypersensitivity. Cross-reactions between various insect antigens are specially considered. Allergy 1978;33:197–202.
Hemmer W, Focke M, Kolarich D, Wilson IB, Altmann F, Wohrl S, Gotz M, Jarisch R: Antibody binding to venom carbohydrates is a frequent cause for double positivity to honeybee and yellow jacket venom in patients with stinging-insect allergy. J Allergy Clin Immunol 2001;108:1045–1052.
Reisman RE, Wypych JI, Lazell MI: Further studies of patients with both honeybee- and yellow-jacket-venom-specific IgE. Int Arch Allergy Appl Immunol 1987;82:190–194.
Straumann F, Bucher C, Wüthrich B: Double sensitization to honeybee and wasp venom: immunotherapy with one or with both venoms? Value of FEIA inhibition for the identification of the cross-reacting IgE antibodies in double-sensitized patients to honeybee and wasp venom. Int Arch Allergy Immunol 2000;123:268–274.
Hemmer W, Focke M, Kolarich D, Dalik I, Gotz M, Jarisch R: Identification by immunoblot of venom glycoproteins displaying immunoglobulin E-binding N-glycans as cross-reactive allergens in honeybee and yellow jacket venom. Clin Exp Allergy 2004;34:460–469.
Jappe U, Raulf-Heimsoth M, Hoffmann M, Burow G, Hubsch-Muller C, Enk A: In vitro Hymenoptera venom allergy diagnosis: improved by screening for cross-reactive carbohydrate determinants and reciprocal inhibition. Allergy 2006;61:1220–1229.
Marz L, Kuhne C, Michl H: The glycoprotein nature of phospholipase A2, hyaluronidase and acid phosphatase from honey-bee venom. Toxicon 1983;21:893–896.
Kubelka V, Altmann F, Marz L: The asparagine-linked carbohydrate of honeybee venom hyaluronidase. Glycoconj J 1995;12:77–83.
Weber A, Schroder H, Thalberg K, Marz L: Specific interaction of IgE antibodies with a carbohydrate epitope of honey bee venom phospholipase A2. Allergy 1987;42:464–470.
Tretter V, Altmann F, Kubelka V, Marz L, Becker WM: Fucose alpha 1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals. Int Arch Allergy Immunol 1993;102:259–266.
King TP, Alagon AC, Kuan J, Sobotka AK, Lichtenstein LM: Immunochemical studies of yellowjacket venom proteins. Mol Immunol 1983;20:297–308.
Hoffman DR, Wood CL: Allergens in Hymenoptera venom. XI. Isolation of protein allergens from Vespula maculifrons (yellow jacket) venom. J Allergy Clin Immunol 1984;74:93–103.
Gmachl M, Kreil G: Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm. Proc Natl Acad Sci USA 1993;90:3569–3573.
King TP, Lu G, Gonzalez M, Qian N, Soldatova L: Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence similarity and antigenic cross-reactivity with their hornet and wasp homologs and possible implications for clinical allergy. J Allergy Clin Immunol 1996;98:588–600.
Skov LK, Seppala U, Coen JJ, Crickmore N, King TP, Monsalve RI, Kastrup JS, Spangfort MD, Gajhede M: Structure of recombinant Ves v 2 at 2.0 Ångstrom resolution: structural analysis of an allergenic hyaluronidase from wasp venom. Acta Crystallogr D Biol Crystallogr 2006;62:595–604.
Markovic-Housley Z, Miglierini G, Soldatova L, Rizkallah PJ, Mueller U, Schirmer T: Crystal structure of hyaluronidase, a major allergen of bee venom. Structure 2000;8:1025–1035.
Hoffman DR, El Choufani SE, Smith MM, de Groot H: Occupational allergy to bumblebees: allergens of Bombus terrestris. J Allergy Clin Immunol 2001;108:855–860.
Hoffman DR, Jacobson RS: Allergens in Hymenoptera venom. XXVII: bumblebee venom allergy and allergens. J Allergy Clin Immunol 1996;97:812–821.
Kochuyt AM, van Hoeyveld EM, Stevens EA: Occupational allergy to bumble bee venom. Clin Exp Allergy 1993;23:190–195.
Hoffman DR, McDonald CA: Allergens in Hymenoptera venom. VII. Species specific reactivity to yellow jacket venoms. Ann Allergy 1981;47:23–27.
Reisman RE, Mueller U, Wypych JI, Elliott W, Arbesman CE: Comparison of the allergenicity and antigenicity of yellow jacket and hornet venoms. J Allergy Clin Immunol 1982;69:268–274.
Reisman RE, Wypych JI, Mueller UR, Grant JA: Comparison of the allergenicity and antigenicity of Polistes venom and other vespid venoms. J Allergy Clin Immunol 1982;70:281–287.
Hoffman DR: Allergens in Hymenoptera venom. XVI. Studies of the structures and cross-reactivities of vespid venom phospholipases. J Allergy Clin Immunol 1986;78:337–343.
Hoffman DR: Allergens in Hymenoptera venom. XXVI. The complete amino acid sequences of two vespid venom phospholipases. Int Arch Allergy Immunol 1994;104:184–190.
Hoffman DR: Allergens in Hymenoptera venom. XXV. The amino acid sequences of antigen 5 molecules and the structural basis of antigenic cross-reactivity. J Allergy Clin Immunol 1993;92:707–716.
Lu G, Villalba M, Coscia MR, Hoffman DR, King TP: Sequence analysis and antigenic cross-reactivity of a venom allergen, antigen 5, from hornets, wasps, and yellow jackets. J Immunol 1993;150:2823–2830.
Henriksen A, King TP, Mirza O, Monsalve RI, Meno K, Ipsen H, Larsen JN, Gajhede M, Spangfort MD: Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily. Proteins 2001;45:438–448.
Didierlaurent A, Foglietti MJ, Guerin B, Hewitt BE, Percheron F: Comparative study on cat allergens from fur and saliva. Int Arch Allergy Appl Immunol 1984;73:27–31.
Viander M, Valovirta E, Vanto T, Koivikko A: Cross-reactivity of cat and dog allergen extracts. RAST inhibition studies with special reference to the allergenic activity in saliva and urine. Int Arch Allergy Appl Immunol 1983;71:252–260.
Guerin B, Hewitt BE: A comparative study of allergen extracts from cat fur, cat pelt and cat saliva. Ann Allergy 1981;46:127–131.
Brown PR, Leitermann K, Ohman L Jr: Distribution of cat allergen 1 in cat tissues and fluids. Int Arch Allergy Appl Immunol 1984;74:67–70.
Hoffman DR: Dog and cat allergens: urinary proteins or dander proteins? Ann Allergy 1980;45:205–206.
Wallenbeck I, Einarsson R: Identification of dander-specific and serum-specific allergens in cat dandruff extract. Ann Allergy 1987;59:131–134.
Martinez A, Martinez J, Sanz ML, Bartolome B, Palacios R: Dander is the best epithelial source for dog allergenic extract preparations. Allergy 1994;49:664–667.
Spitzauer S, Schweiger C, Sperr WR, Pandjaitan B, Valent P, Muhl S, Ebner C, Scheiner O, Kraft D, Rumpold H: Molecular characterization of dog albumin as a cross-reactive allergen. J Allergy Clin Immunol 1994;93:614–627.
Spitzauer S, Pandjaitan B, Muhl S, Ebner C, Kraft D, Valenta R, Rumpold H: Major cat and dog allergens share IgE epitopes. J Allergy Clin Immunol 1997;99:100–106.
Goubran Botros H, Gregoire C, Rabillon J, David B, Dandeu JP: Cross-antigenicity of horse serum albumin with dog and cat albumins: study of three short peptides with significant inhibitory activity towards specific human IgE and IgG antibodies. Immunology 1996;88:340–347.
Smith WA, Butler AJ, Hazell LA, Chapman MD, Pomes A, Nickels DG, Thomas WR: Fel d 4, a cat lipocalin allergen. Clin Exp Allergy 2004;34:1732–1738.
Boutin Y, Hebert H, Vrancken ER, Mourad W: Allergenicity and cross-reactivity of cat and dog allergenic extracts. Clin Allergy 1988;18:287–293.
Wüthrich B, Guerin B, Hewitt BE: Cross-allergenicity between extracts of hair from different dog breeds and cat fur. Clin Allergy 1985;15:87–93.
Ohman L Jr, Bloch KJ, Kendall S, Lowell FC: Allergens of mammalian origin. IV. Evidence for common allergens in cat and dog serum. J Allergy Clin Immunol 1976;57:560–568.
Mari A: Importance of databases in experimental and clinical allergology. Int Arch Allergy Immunol 2005;138:88–96.
Boluda L, Alonso C, Fernandez-Caldas E: Purification, characterization, and partial sequencing of two new allergens of Olea europaea. J Allergy Clin Immunol 1998;101:210–216.
Batanero E, Ledesma A, Villalba M, Rodriguez R: Purification, amino acid sequence and immunological characterization of Ole e 6, a cysteine-enriched allergen from olive tree pollen. FEBS Lett 1997;410:293–296.
Midoro-Horiuti T, Goldblum RM, Kurosky A, Wood TG, Brooks EG: Variable expression of pathogenesis-related protein allergen in mountain cedar (Juniperus ashei) pollen. J Immunol 2000;164:2188–2192.
Bose R, Ekramoddoullah AK, Kisil FT, Sehon AH: Human and murine antibodies to rye grass pollen allergen Lol p IV share a common idiotope. Immunology 1988;63:579–584.
Vrtala S, Fischer S, Grote M, Vangelista L, Pastore A, Sperr WR, Valent P, Reichelt R, Kraft D, Valenta R: Molecular, immunological, and structural characterization of Phl p 6, a major allergen and P-particle-associated protein from Timothy grass (Phleum pratense) pollen. J Immunol 1999;163:5489–5496.
Ansari AA, Killoran EA, Marsh DG: An investigation of human immune response to perennial ryegrass (Lolium perenne) pollen cytochrome c (Lol p X). J Allergy Clin Immunol 1987;80:229–235.
Marknell DeWitt A, Niederberger V, Lehtonen P, Spitzauer S, Sperr WR, Valent P, Valenta R, Lidholm J: Molecular and immunological characterization of a novel timothy grass (Phleum pratense) pollen allergen, Phl p 11. Clin Exp Allergy 2002;32:1329–1340.
van Ree R, Hoffman DR, van Dijk W, Brodard V, Mahieu K, Koeleman CA, Grande M, van Leeuwen WA, Aalberse RC: 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.
Petersen A, Suck R, Hagen S, Cromwell O, Fiebig H, Becker WM: Group 13 grass allergens: structural variability between different grass species and analysis of proteolytic stability. J Allergy Clin Immunol 2001;107:856–862.
Nilsen BM, Grimsoen A, Paulsen BS: Identification and characterization of important allergens from mugwort pollen by IEF, SDS-PAGE and immunoblotting. Mol Immunol 1991;28:733–742.
Nilsen BM, Paulsen BS: Isolation and characterization of a glycoprotein allergen, Art v II, from pollen of mugwort (Artemisia vulgaris L.). Mol Immunol 1990;27:1047–1056.
Atassi H, Atassi MZ: Antibody recognition of ragweed allergen Ra3: localization of the full profile of the continuous antigenic sites by synthetic overlapping peptides representing the entire protein chain. Eur J Immunol 1986;16:229–235.
Goodfriend L, Choudhury AM, Klapper DG, Coulter KM, Dorval G, del Carpio J, Osterland CK: Ra5G, a homologue of Ra5 in giant ragweed pollen: isolation, HLA-DR-associated activity and amino acid sequence. Mol Immunol 1985;22:899–906.
Giuliani A, Pini C, Bonini S, Mucci N, Ferroni L, Vicari G: Isolation and purification of a major allergen from Parietaria officinalis pollen. Allergy 1987;42:434–440.
Duro G, Colombo P, Costa MA, Izzo V, Porcasi R, di Fiore R, Locorotondo G, Mirisola MG, Cocchiara R, Geraci D: cDNA cloning, sequence analysis and allergological characterization of Par j 2.0101, a new major allergen of the Parietaria judaica pollen. FEBS Lett 1996;399:295–298.
Ayuso R, Carreira J, Polo F: Quantitation of the major allergen of several Parietaria pollens by an anti-Par 1 monoclonal antibody-based ELISA. Analysis of crossreactivity among purified Par j 1, Par o 1 and Par m 1 allergens. Clin Exp Allergy 1995;25:993–999.
Bonura A, Gulino L, Trapani A, di Felice G, Tinghino R, Amoroso S, Geraci D, Valenta R, Westritschnig K, Scala E, Mari A, Colombo P: Isolation, expression and immunological characterization of a calcium-binding protein from Parietaria pollen. Mol Immunol 2008;45:2465–2473.
Costa MA, Colombo P, Izzo V, Kennedy H, Venturella S, Cocchiara R, Mistrello G, Falagiani P, Geraci D: cDNA cloning, expression and primary structure of Par j I, a major allergen of Parietaria judaica pollen. FEBS Lett 1994;341:182–186.
Lake FR, Ward LD, Simpson RJ, Thompson PJ, Stewart GA: House dust mite-derived amylase: allergenicity and physicochemical characterization. J Allergy Clin Immunol 1991;87:1035–1042.
Le Mao J, Mayer CE, Peltre G, Desvaux FX, David B, Weyer A, Senechal H: Mapping of Dermatophagoides farinae mite allergens by two-dimensional immunoblotting. J Allergy Clin Immunol 1998;102:631–636.
Yasueda H, Mita H, Akiyama K, Shida T, Ando T, Sugiyama S, Yamakawa H: Allergens from Dermatophagoides mites with chymotryptic activity. Clin Exp Allergy 1993;23:384–390.
O’Neil SE, Heinrich TK, Hales BJ, Hazell LA, Holt DC, Fischer K, Thomas WR: The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus. Clin Exp Allergy 2006;36:831–839.
Entrez Protein – National Institutes of Health (NIH) protein sequence database.
Thomas WR, Smith WA, Hales BJ, Mills KL, O’Brien RM: Characterization and immunobiology of house dust mite allergens. Int Arch Allergy Immunol 2002;129:1–18.
Binder M, Fierlbeck G, King TP, Valent P, Buhring HJ: Individual Hymenoptera venom compounds induce upregulation of the basophil activation marker ectonucleotide pyrophosphatase/phosphodiesterase 3 (CD203c) in sensitized patients. Int Arch Allergy Immunol 2002;129:160–168.
Hoffman DR: Allergens in Hymenoptera venom XIV: IgE binding activities of venom proteins from three species of vespids. J Allergy Clin Immunol 1985;75:606–610.
Winningham KM, Fitch CD, Schmidt M, Hoffman DR: Hymenoptera venom protease allergens. J Allergy Clin Immunol 2004;114:928–933.
Virtanen T, Jarvi RM: Mammalian allergens. Clin Allergy Immunol 2004;18:297–317.
Saarelainen S, Taivainen A, Rytkonen-Nissinen M, Auriola S, Immonen A, Mantyjarvi R, Rautiainen J, Kinnunen T, Virtanen T: Assessment of recombinant dog allergens Can f 1 and Can f 2 for the diagnosis of dog allergy. Clin Exp Allergy 2004;34:1576–1582.
Ichikawa K, Vailes LD, Pomes A, Chapman MD: Molecular cloning, expression and modelling of cat allergen, cystatin (Fel d 3), a cysteine protease inhibitor. Clin Exp Allergy 2001;31:1279–1286.
Adedoyin J, Johansson SG, Gronlund H, van Hage M: Interference in immunoassays by human IgM with specificity for the carbohydrate moiety of animal proteins. J Immunol Methods 2006;310:117–125.
Copyright / Drug Dosage / Disclaimer
Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher.
Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.
You do not currently have access to this content.