Cited by 393Glycosylation and Glycoproteins ResearchAllergic Rhinitis and SensitizationFood Allergy and Anaphylaxis Research

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The Role of Protein Glycosylation in Allergy

Altmann, Friedrich·2007·International Archives of Allergy and Immunology

DOI 10.1159/000096114

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Abstract

The asparagine-linked carbohydrate moieties of plant and insect glycoproteins are the most abundant environmental immune determinants. They are the structural basis of what is known as cross-reactive carbohydrate determinants (CCDs). Despite some structural variation, the two main motifs are the xylose and the core-3-linked fucose, which form the essential part of two independent epitopes. Plants contain both epitopes, insect glycoproteins only fucose. These epitopes and other fucosylated determinants are also found in helminth parasites where they exert remarkable immunomodulatory effects. About 20% or more of allergic patients generate specific anti-glycan IgE, which is often accompanied by IgG. Even though antibody-binding glycoproteins are widespread in pollens, foods and insect venoms, CCDs do not appear to cause clinical symptoms in most, if not all patients. When IgE binding is solely due to CCDs, a glycoprotein allergen thus can be rated as clinical irrelevant allergen. Low binding affinity between IgE and plant N-glycans now drops out as a plausible explanation for the benign nature of CCDs. This rather may result from blocking antibodies induced by an incidental ‘immune therapy’ (‘glyco-specific immune therapy’) exerted by everyday contact with plant materials, e.g. fruits or vegetables. The need to detect and suppress anti-CCD IgE without interference from peptide epitopes can be best met by artificial glycoprotein allergens. Hydroxyproline-linked arabinose (single β-arabinofuranosyl residues) has been identified as a new IgE-binding carbohydrate epitope in the major mugwort allergen. However, currently the occurrence of this O-glycan determinant appears to be rather restricted.

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10.1016%2F0091-6749%2881%2990133-0 · DOI
10.1016%2FS0091-6749%2897%2970245-8 · DOI
10.1097%2F00130832-200406000-00017 · DOI
10.1111%2Fj.1365-2222.2004.01837.x · DOI
10.1111%2Fj.1365-2222.2005.02217.x · DOI
10.1111%2Fj.1398-9995.1995.tb01202.x · DOI
10.1111%2Fj.1365-2222.2005.02294.x · DOI
10.1067%2Fmai.2001.116430 · DOI
10.1159%2F000067591 · DOI
10.1067%2Fmai.2003.1683 · DOI
10.1046%2Fj.1398-9995.2003.00407.x · DOI · Paper page
10.1067%2Fmai.2002.126380 · DOI
10.1007%2FBF01108609 · DOI
10.1093%2Fglycob%2F8.7.651 · DOI
10.1093%2Fglycob%2F11.4.261 · DOI · Paper page
10.1023%2FA%3A1006012005654 · DOI
10.1074%2Fjbc.M410407200 · DOI
10.1111%2Fj.1398-9995.1987.tb00364.x · DOI
10.1159%2F000236534 · DOI
10.2174%2F1389201003378843 · DOI
10.1016%2FS0959-440X%2802%2900367-6 · DOI
10.1016%2FS0300-9084%2801%2901297-4 · DOI
10.1055%2Fs-2003-44721 · DOI
10.1023%2FA%3A1006960401562 · DOI
10.1271%2Fbbb.69.137 · DOI
10.1271%2Fbbb.69.1700 · DOI
10.1016%2FS0008-6215%2800%2990610-4 · DOI
10.1111%2Fj.1432-1033.1987.tb13517.x · DOI
10.1515%2FBC.2004.044 · DOI
10.1046%2Fj.1432-1033.2003.03503.x · DOI
10.1074%2Fjbc.275.15.11451 · DOI
10.1006%2Fabio.2000.4737 · DOI
10.1042%2FBJ20041062 · DOI
10.1111%2Fj.1742-4658.2005.05000.x · DOI
10.1074%2Fjbc.271.43.26653 · DOI
10.1111%2Fj.1365-2222.2004.01897.x · DOI
10.1007%2FBF00731872 · DOI
10.1111%2Fj.1432-1033.1993.tb17870.x · DOI
10.1093%2Fglycob%2F4.2.105 · DOI
10.1111%2Fj.1742-4658.2005.04841.x · DOI
10.1093%2Fglycob%2F11.2.149 · DOI
10.1093%2Fglycob%2F7.5.653 · DOI
10.1016%2FS0014-5793%2899%2901508-2 · DOI
10.1074%2Fjbc.271.48.30561 · DOI
10.1111%2Fj.1432-1033.1995.tb20809.x · DOI
10.1111%2Fj.1432-1033.2004.04045.x · DOI
10.1111%2Fj.1432-1033.1997.00195.x · DOI
10.1016%2FS0014-5793%2899%2901489-1 · DOI
10.1111%2Fj.1365-3024.2005.00781.x · DOI
10.1016%2Fj.ijpara.2004.04.009 · DOI
10.1016%2Fj.bmc.2005.02.009 · DOI
10.1111%2Fj.1742-4658.2005.05068.x · DOI
10.1017%2FS0031182004006390 · DOI
10.1074%2Fjbc.M505985200 · DOI
10.1111%2Fj.0105-2896.2004.00187.x · DOI
10.1128%2FIAI.72.1.398-407.2004 · DOI
10.1002%2Feji.200323717 · DOI · Paper page
10.1016%2FS0198-8859%2899%2900136-6 · DOI
10.1126%2Fscience.296.5567.490 · DOI
10.1007%2FBF01049085 · DOI
10.1016%2F0300-9084%2888%2990285-4 · DOI
10.1006%2Fabio.1993.1088 · DOI
10.1016%2FS0091-6749%2896%2970130-6 · DOI
10.1093%2Fglycob%2Fcwh058 · DOI
10.1021%2Fbi00025a027 · DOI
10.1111%2Fj.1432-1033.1990.tb15553.x · DOI
10.1093%2Fglycob%2Fcwj071 · DOI
10.1093%2Fglycob%2Fcwg024 · DOI
10.1111%2Fj.1398-9995.1998.tb03934.x · DOI
10.1046%2Fj.1365-2222.2001.01019.x · DOI
10.1007%2FBF00393072 · DOI
10.1093%2Fglycob%2Fcwg025 · DOI · Paper page
10.1016%2Fj.micron.2003.10.033 · DOI
10.1046%2Fj.1365-2222.1999.00590.x · DOI
10.1016%2FS0091-6749%2899%2970538-5 · DOI
10.1023%2FA%3A1014860030380 · DOI · Paper page
10.1067%2Fmai.2001.120013 · DOI
10.1046%2Fj.1365-2222.2002.01516.x · DOI
10.1111%2Fj.1365-2222.2005.02371.x · DOI
10.1159%2F000024404 · DOI
10.1159%2F000090384 · DOI
10.1159%2F000065180 · DOI
10.1016%2Fj.jaci.2004.11.020 · DOI
10.1034%2Fj.1398-9995.2002.23686.x · DOI
10.1034%2Fj.1398-9995.2002.13423.x · DOI
10.1046%2Fj.1365-2222.2002.01530.x · DOI
10.1111%2Fj.1365-2222.2004.1948.x · DOI
10.1111%2Fj.1398-9995.1998.tb03813.x · DOI
10.1067%2Fmai.2000.108711 · DOI
10.1067%2Fmai.2003.173 · DOI
10.1046%2Fj.1432-1327.1998.2520118.x · DOI
10.1159%2F000066770 · DOI
10.1006%2Fabio.1999.4277 · DOI
10.1159%2F000073260 · DOI
10.1172%2FJCI25575 · DOI
10.1016%2Fj.jaci.2004.03.024 · DOI
10.1159%2F000236835 · DOI
10.1159%2F000091169 · DOI
10.1159%2F000023996 · DOI
10.1515%2FCCLM.2006.024 · DOI
10.1111%2Fj.1365-2222.2006.2492.x · DOI
10.1016%2Fj.ymeth.2003.08.018 · DOI
10.1515%2FCCLM.2005.226 · DOI
10.1067%2Fmai.2003.1495 · DOI
10.1002%2Feji.1830250235 · DOI
10.1016%2Fj.jim.2006.01.001 · DOI

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Background
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Background
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Background
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Toward Stable Genetic Engineering of Human O-Glycosylation in Plants1[C][W][OA]
Yang, Z., Bennett, E., Jørgensen, B., Drew, D., Arigi, E., Mandel, U., Ulvskov, P., Levery, S., Clausen, H., & Petersen, B. (2012) · Plant Physiology · doi:10.1104/pp.112.198200 · Cited by 28
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“Indeed, the immunogenicity of some of these identified glycans have been reported in human and mouse models [47, 48].”
Background
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BackgroundResultInfluential
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Background
Role of the polypeptide backbone and post-translational modifications in cross-reactivity of Art v 1, the major mugwort pollen allergen
Gruber, P., Gadermaier, G., Bauer, R., Weiss, R., Wagner, S., Léonard, R., Breiteneder, H., Ebner, C., Ferreira, F., & Egger, M. (2009) · Biological chemistry · doi:10.1515/bc.2009.063 · Cited by 27
“Thus, the overall impression is that carbohydrate-specific IgE antibodies are of poor biological activity, and their clinical relevance is doubted (Mari et al., 1999; Malandain, 2005; Altmann, 2007).”
Background
A review of the safety evidence on recombinant human lactoferrin for use as a food ingredient
Vishwanath-Deutsch, R., Dallas, D. C., Besada‐Lombana, P. B., Katz, L., Conze, D. B., Kruger, C. L., Clark, A. J., Peterson, R., & Malinczak, C. (2024) · Food and Chemical Toxicology · doi:10.1016/j.fct.2024.114727 · Cited by 28
Tomato Allergy: The Characterization of the Selected Allergens and Antioxidants of Tomato (Solanum lycopersicum)—A Review
Włodarczyk, K., Smolińska, B., & Majak, I. (2022) · Antioxidants · doi:10.3390/antiox11040644 · Cited by 26
“The research of Fredrich Altmann (2007) [85] found that at least 20% of allergic patients generate specific anti-glycan IgE, which is often accompanied by IgG.”
Background
Main Strategies of Plant Expression System Glycoengineering for Producing Humanized Recombinant Pharmaceutical Proteins
Rozov, S. M., Permyakova, N. V., & Deineko, E. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918030033 · Cited by 26
Allergy to kiwi in patients with baker's asthma: identification of potential cross-reactive allergens.
Palacín, A., Quirce, S., Sánchez-Monge, R., Fernández-Nieto, M., Varela, J., Sastre, J., & Salcedo, G. (2008) · Annals of Allergy, Asthma & Immunology · doi:10.1016/s1081-1206(10)60210-4 · Cited by 26
Molecular and immunological characterisation of the glycosylated orange allergen Cit s 1
Pöltl, G., Ahrazem, O., Paschinger, K., Ibáñez, M. D., Salcedo, G., & Wilson, I. B. H. (2006) · Glycobiology · doi:10.1093/glycob/cwl068 · Cited by 26
“On the other hand, the matter as to whether cross-reactive carbohydrate epitopes are clinically significant has been a matter of controversy and debate (Aalberse and Van Ree 1997; Van der Veen et al. 1997; Fötisch and Vieths 2001; Altmann 2007).”
Developments in the production of mucosal antibodies in plants
Vasilev, N. P., Smales, C. M., Schillberg, S., Fischer, R., & Schiermeyer, A. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.11.002 · Cited by 28
The crux with a reliable in vitro and in vivo diagnosis of allergy
Crameri, R. (2013) · Allergy. European Journal of Allergy and Clinical Immunology · doi:10.1111/all.12177 · Cited by 25
“Even though antibody-binding glycoproteins are widespread in many extracts, CCDs do not appear to cause clinical symptoms in most, if not all, patients and can thus be considered as clinically irrelevant allergens (12).”
Background
Assessment of the potential allergenicity of genetically-engineered food crops
Ladics, G. (2018) · Journal of Immunotoxicology · doi:10.1080/1547691x.2018.1533904 · Cited by 24
Glycan Microarray-Assisted Identification of IgG Subclass Targets in Schistosomiasis
Yang, Y. Y. M., van Diepen, A., Brzezicka, K., Reichardt, N., & Hokke, C. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02331 · Cited by 24
“Interestingly, although we have not observed very high IgG4 binding intensities against schistosome glycans, precisely the core α3-fucose and core xylose motifs that form the cross-reactive carbohydrate determinants for IgE in plant allergens as well as helminths (28, 33, 36) are also the only IgG4 reactive glycan ele…”
Background
Specific Antibodies for the Detection of Alternaria Allergens and the Identification of Cross-Reactive Antigens in Other Fungi
Twaroch, T., Curin, M., Sterflinger, K., Focke‐Tejkl, M., Swoboda, I., & Valenta, R. (2016) · International Archives of Allergy and Immunology · doi:10.1159/000449415 · Cited by 24
“The recognition by allergen-specific antibodies and, in particular, antibody probes specific for the protein backbone of the allergen, is not affected by cross-reactive carbohydrates coupled to various allergens [22].”
Background
Impact of arbuscular mycorrhizal fungi on the allergenic potential of tomato
Schwarz, D., Welter, S., George, E., Franken, P., Lehmann, K., Weckwerth, W., Dölle, S., & Worm, M. (2011) · Mycorrhiza · doi:10.1007/s00572-010-0345-z · Cited by 24
“This could be based on translational control or posttranslational modifications of the corresponding proteins which are important for their allergenic potential (Altmann 2007; Ballmer-Weber et al. 2002).”
Background
Process Optimization for Recombinant Protein Expression in Insect Cells
Zitzmann, J., Sprick, G., Weidner, T., Schreiber, C., & Czermak, P. (2017) · InTech eBooks · doi:10.5772/67849 · Cited by 24
“In addition to human-like α1,6-linked fucose, insect-derived proteins may also carry a α1,3-linked fucose, which can induce immunogenic and allergic responses in humans [14].”
Background
Involvement of cross-reactive carbohydrate determinants-specific IgE in pollen allergy testing
Yokoi, H., Yoshitake, H., Matsumoto, Y., Kawada, M., Takato, Y., Shinagawa, K., Sakurai, H., & Saito, K. (2017) · Asia Pacific Allergy · doi:10.5415/apallergy.2017.7.1.29 · Cited by 23
Minimizing fucosylation in insect cell-derived glycoproteins reduces binding to IgE antibodies from the sera of patients with allergy
Palmberger, D., Ashjaei, K., Strell, S., Hoffmann-Sommergruber, K., & Grabherr, R. (2014) · Biotechnology Journal · doi:10.1002/biot.201400061 · Cited by 23
Determination of sIgE to rPhl p 1 is sufficient to diagnose grass pollen allergy
Bokanovic, D., Aberer, W., Hemmer, W., Heinemann, A., Komericki, P., Scheffel, J., & Sturm, G. (2013) · Allergy. European Journal of Allergy and Clinical Immunology · doi:10.1111/all.12263 · Cited by 23
“Phl p 1, Phl p 4, Phl p 11, and Phl p 13 are known to be glycosylated (19, 20), so if antibodies against CCDs are present in the serum, patients should be false positive for the natural extract of timothy grass, but not for the CCD-free recombinant Phl p 1.”
Background
Minor Interference of Cross-Reactive Carbohydrates with the Diagnosis of Respiratory Allergy in Standard Clinical Conditions
Vidal, C., Sanmartín, C., Armisén, M., Rodríguez, V., Linneberg, A., & González-Quintela, A. (2011) · International Archives of Allergy and Immunology · doi:10.1159/000324447 · Cited by 23
Kreuzreaktivität auf Bienen- und Wespengift
Hemmer, W. (2008) · Der Hautarzt · doi:10.1007/s00105-008-1485-3 · Cited by 23
Complex N-Glycans Are Important for Normal Fruit Ripening and Seed Development in Tomato
Kaulfürst-Soboll, H., Mertens-Beer, M., Brehler, R., Albert, M., & von Schaewen, A. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.635962 · Cited by 28
“Based on their ability to be bound by specific immunoglobulin E (IgE) antibodies, regardless of the origin, they appear to react similarly to pan-allergens, although in this case without clinical symptoms (Aalberse et al., 1981; reviewed by Altmann, 2007).”
Background
The History of Carbohydrates in Type I Allergy
Hils, M., Wölbing, F., Hilger, C., Fischer, J., Hoffard, N., & Biedermann, T. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.586924 · Cited by 25
“The initial steps of protein N-glycosylation are essentially conserved in all eukaryotic organisms (9, 25), however, the following steps differ between ‘higher animals’, i.”
BackgroundInfluential
Insect allergens on the dining table.
Jeong, K., & Park, J. (2020) · Current protein and peptide science · doi:10.2174/1389203720666190715091951 · Cited by 22
IgE antibodies in occupational asthma: are they causative or an associated phenomenon?
Quirce, S. (2014) · Current Opinion in Allergy and Clinical Immunology · doi:10.1097/aci.0000000000000041 · Cited by 22
The role of N-glycosylation in kiwi allergy
Garrido-Arandía, M., Murua-García, A., Palacín, A., Tordesillas, L., Gómez-Casado, C., Blanca-López, N., Ramos, T., Cantó, G., Blanco, C., Cuesta-Herranz, J., et al. (2014) · Food Science & Nutrition · doi:10.1002/fsn3.99 · Cited by 22
“This N-complex glycan, highly enriched in mannose, has been associated with Th2 responses (Altmann 2007).”
BackgroundInfluential
Cross-reacting carbohydrate determinants and hymenoptera venom allergy
Brehler, R., Grundmann, S., & Stöcker, B. (2013) · Current Opinion in Allergy and Clinical Immunology · doi:10.1097/aci.0b013e328362c544 · Cited by 22
“A suggested mechanism explaining the clinical insignificance of CCDs is a comparably high IgG affinity and a not too high titer of CCD-IgE.”
BackgroundInfluential
Mucin-type proteins produced in the Trichoplusia ni and Spodoptera frugiperda insect cell lines carry novel O-glycans with phosphocholine and sulfate substitutions.
Gaunitz, S., Jin, C., Nilsson, A., Liu, J.-N., Karlsson, N., & Holgersson, J. (2013) · Glycobiology · doi:10.1093/glycob/cwt015 · Cited by 22
“core α1,3-Fuc) (van Die and Cummings 2006; Altmann 2007; Harnett et al. 2008).”
Background
Silencing ?1,2-xylosyltransferase in Transgenic Tomato Fruits Reveals xylose as Constitutive Component of Ige-Binding Epitopes
Paulus, K. E., Mahler, V., Pabst, M., Kogel, K., Altmann, F., & Sonnewald, U. (2011) · Frontiers in Plant Science · doi:10.3389/fpls.2011.00042 · Cited by 25
“They are regarded as the major class of the so-called “carbohydrate cross-reactive determinants” (CCDs; Wilson and Altmann, 1998) reactive with IgE antibodies in the sera of many allergic patients (Strasser et al., 2004), however their clinical relevance is still under debate. Structurally similar CCDs are present in…”
BackgroundMethodInfluentialSelf-citation
The N-glycans of Chlorella sorokiniana and a related strain contain arabinose but have strikingly different structures
Mócsai, R. T., Blaukopf, M. K., Svehla, E., Kosma, P., & Altmann, F. (2020) · Glycobiology · doi:10.1093/glycob/cwaa012 · Cited by 28
Self-citation
Cross-Reactivity between Oak and Birch Pollens in Korean Tree Pollinosis
Jeong, K., Son, M., Park, J.-H., Park, K., Park, H., Lee, J.-H., Hong, C., & Park, J.-W. (2016) · Journal of Korean medical science · doi:10.3346/jkms.2016.31.8.1202 · Cited by 21
“In addition, cross-reactive carbohydrate determinants are also known to cause in vitro IgE reactivity even though they do not induce clinical symptoms (16).”
Background
Purification and Characterization of the Major Oak Pollen Allergen Que a 1 for Component-Resolved Diagnostics Using ImmunoCAP®
Movérare, R., Everberg, H., Carlsson, R., Holtz, A., Thunberg, R., Olsson, P., Brostedt, P., & Högbom, E. (2008) · International Archives of Allergy and Immunology · doi:10.1159/000115888 · Cited by 21
“The preserved immunoreactivity of nQue a 1 was shown by specific IgE inhibition, and 2D PAGE indicated that our nQue a 1 preparation was composed of at least five different isoforms.Experimental nQue a 1 ImmunoCAP was developed. No binding of monoclonal or polyclonal mouse antibodies directed to profilins or calcium-b…”
A plant-produced SARS-CoV-2 spike protein elicits heterologous immunity in hamsters
Margolin, E., Schäfer, G., Allen, J., Gers, S., Woodward, J., Sutherland, A. D., Blumenthal, M. J., Meyers, A., Shaw, M., Preiser, W., et al. (2023) · Frontiers in Plant Science · doi:10.3389/fpls.2023.1146234 · Cited by 20
“Foreign glyco-epitopes have been associated with hypersensitive reactions and some plant glycoproteins are allergens (Altmann, 2007; Arnold and Misbah, 2008); however, plant-speci ﬁ c glycosylation has been shown to be safe in volunteers immunized with plant-derived VLPs (Ward et al., 2014; Ward et…”
Recombinant glycoproteins resembling carbohydrate-specific IgE epitopes from plants, venoms and mites
Gattinger, P., Mittermann, I., Lupinek, C., Hofer, G., Keller, W., Bidovec-Stojkovič, U., Korošec, P., Koessler, C., Novak, N., & Valenta, R. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.12.002 · Cited by 20
“Plant, venom and mite-derived alpha 1,3-core-fucose is not found on human proteins [3] but crossreactivity had been reported in pollen, fruits and vegetables, [4,5] insect”
Background
Identification of dominant anti-glycan IgE responses in school children by glycan microarray
Amoah, A., Asuming-Brempong, E., Obeng, B., Versteeg, S., Larbi, I. A., Aryeetey, Y., Platts-Mills, T., Mari, A., Brzezicka, K., Gyan, B., et al. (2017) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2017.09.040 · Cited by 20
Mimotopes for Api g 5, a Relevant Cross-reactive Allergen, in the Celery-Mugwort-Birch-Spice Syndrome
Lukschal, A., Wallmann, J., Bublin, M., Hofstetter, G., Mothes-Luksch, N., Breiteneder, H., Pali-Schöll, I., & Jensen-Jarolim, E. (2015) · Allergy Asthma and Immunology Research · doi:10.4168/aair.2016.8.2.124 · Cited by 20
Interfaces Between Allergen Structure and Diagnosis: Know Your Epitopes
Pomés, A., Chruszcz, M., Gustchina, A., & Wlodawer, A. (2015) · Current Allergy and Asthma Reports · doi:10.1007/s11882-014-0506-9 · Cited by 20
Systemic and mucosal IgE antibody responses of horses to infection with Anoplocephala perfoliata.
Pittaway, C. E., Lawson, A., Coles, G., & Wilson, A. (2014) · Veterinary parasitology · doi:10.1016/j.vetpar.2013.10.005 · Cited by 20
Differential Patterns of Liver Proteins in Experimental Murine Hepatosplenic Schistosomiasis
Manivannan, B., Rawson, P., Jordan, T., Secor, W., & Flamme, A. L. L. (2009) · Infection and Immunity · doi:10.1128/iai.00647-09 · Cited by 20
Impact of Protein Glycosylation on the Design of Viral Vaccines.
Schön, K., Lepenies, B., & Goyette-Desjardins, G. (2020) · Advances in Biochemical Engineering/Biotechnology · doi:10.1007/10_2020_132 · Cited by 19
Cross-reactive carbohydrate determinant-specific IgE obscures true atopy and exhibits α-1,3-fucose epitope-specific inverse associations with asthma
Nkurunungi, G., Mpairwe, H., Versteeg, S., van Diepen, A., Nassuuna, J., Kabagenyi, J., Nambuya, I., Sanya, R., Nampijja, M., Serna, S., et al. (2020) · Allergy. European Journal of Allergy and Clinical Immunology · doi:10.1111/all.14469 · Cited by 19
“Age in years, median (IQR) 28 (21, 36) 22 (10, 32) .”
Identification and Characterization of β-Lathyrin, an Abundant Glycoprotein of Grass Pea ( Lathyrus sativus L.), as a Potential Allergen.
Xu, Q.-L., Song, B., Liu, F.-J., Song, Y.-Q., Chen, P., Liu, S.-S., & Krishnan, H. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b02314 · Cited by 19
Synthetic plant glycans.
Pfrengle, F. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.09.010 · Cited by 19
Pla a 2 and Pla a 3 reactivities identify plane tree‐allergic patients with respiratory symptoms or food allergy
Scala, E., Cecchi, L., Abeni, D., Guerra, E., Pirrotta, L., Locanto, M., Giani, M., & Asero, R. (2017) · Allergy. European Journal of Allergy and Clinical Immunology · doi:10.1111/all.13121 · Cited by 19
“One hundred and seventy-five participants, both Pla a 2 monoreactors- and MUXF3-positive, were excluded from the study because of CCD reactors, and non-plane tree-allergic patients as further confirmed by negative skin prick test for plane tree extracts (7).”
Background
Structural characterization of a Vatairea macrocarpa lectin in complex with a tumor-associated antigen: A new tool for cancer research.
Sousa, B. L., Silva-Filho, J. C., Kumar, P., Graewert, M., Pereira, R. I., Cunha, R. M., Nascimento, K., Bezerra, G., Delatorre, P., Djinović-Carugo, K., et al. (2016) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2015.12.016 · Cited by 19
The potential of Physcomitrella patens as a platform for the production of plant-based vaccines
Rosales-Mendoza, S., Orellana-Escobedo, L., Romero-Maldonado, A., Decker, E., & Reski, R. (2014) · Expert Review of Vaccines · doi:10.1586/14760584.2014.872987 · Cited by 19
“Some undesired effects are also a possibility as these fucose and xylose residues can mediate the development of allergies through the binding of anti-IgE, especially when considering the correlation between IgE levels responsible for immunoreactivity to carbohydrate compounds and allergic disorders [60,61].”
Background
Immunoglobulin-E reactivity to a glycosylated food allergen (peanuts) due to interference with cross-reactive carbohydrate determinants in heavy drinkers.
Vidal, C., Vizcaíno, L., Díaz-Peromingo, J., Garrido, M., Gómez-Rial, J., Linneberg, A., & González-Quintela, A. (2009) · Alcoholism: Clinical and Experimental Research · doi:10.1111/j.1530-0277.2009.00961.x · Cited by 19
Plant-Made Antibodies: Properties and Therapeutic Applications.
Komarova, T., Шешукова, Е. В., & Dorokhov, Y. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867325666171212093257 · Cited by 19
Allergenic Properties and Molecular Characteristics of PR-1 Proteins
Wangorsch, A., Scheurer, S., Blanca, M., Blanca-López, N., Somoza, M. L., & Martín-Pedraza, L. (2022) · Frontiers in Allergy · doi:10.3389/falgy.2022.824717 · Cited by 18
“Moreover, Cyn d 24 and other glycoproteins fromBermuda grass pollen carry non-xylosylated glycans, mainly MMF3, which are also found in insect venom (26).”
Background
Microarray assessment of N-glycan-specific IgE and IgG profiles associated with Schistosoma mansoni infection in rural and urban Uganda
Nkurunungi, G., van Diepen, A., Nassuuna, J., Sanya, R., Nampijja, M., Nambuya, I., Kabagenyi, J., Serna, S., Reichardt, N., van Ree, R., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40009-7 · Cited by 18
Six years of INSTAND e. V. sIgE proficiency testing
Wojtalewicz, N., Goseberg, S., Kabrodt, K., & Schellenberg, I. (2017) · Allergo Journal International · doi:10.1007/s40629-016-0005-8 · Cited by 18
Allergen-Associated Immunomodulators: Modifying Allergy Outcome
Gómez‐Casado, C., & Díaz‐Perales, A. (2016) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-016-0401-2 · Cited by 17
“Many of the C type lectin-like receptors that are found on DCs function as antigen uptake receptors, including mannose receptor (MR; CD206), DCSIGN (CD209), and DEC-205 (CD205) (Altmann 2007).”
BackgroundInfluential
In-Depth Glycoproteomic Characterization of γ-Conglutin by High-Resolution Accurate Mass Spectrometry
Schiarea, S., Arnoldi, L., Fanelli, R., de Combarieu, E., & Chiabrando, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073906 · Cited by 18
“Glycoproteins with these glyco-epitopes (known as Cross-reactive Carbohydrate Determinants, CCDs) [51], can elicit the production of antibodies in humans that, being specific for the carbohydrate target but not for the carrier proteins, can easily cross-react in in vitro allergy tests with non-homologous (but CCD-carr…”
Background
Optimisation and Use of Humanised RBL NF-AT-GFP and NF-AT-DsRed Reporter Cell Lines Suitable for High-Throughput Scale Detection of Allergic Sensitisation in Array Format and Identification of the ECM–Integrin Interaction as Critical Factor
Wang, X.-W., Cato, P., Lin, H.-C., Li, T., Wan, D., Alcocer, M., & Falcone, F. H. (2013) · Molecular Biotechnology · doi:10.1007/s12033-013-9689-x · Cited by 18
“engage surface-bound IgE productively on mast cells and basophils, and are thus often clinically irrelevant [8, 9].”
Background
N-Glycosylation and N-Glycan Moieties of CTB Expressed in Rice Seeds
Kajiura, H., Wasai, M., Kasahara, S., Takaiwa, F., & Fujiyama, K. (2013) · Molecular Biotechnology · doi:10.1007/s12033-012-9626-4 · Cited by 18
“Furthermore, b1,2-xylose and a1,3-fucose residues are considered as a IgE-binding carbohydrate determinants, the so-called cross-reactive carbohydrate determinants of plant allergens [29, 30].”
Background
Immunoglobulin E Sensitization to Cross-Reactive Carbohydrate Determinants: Epidemiological Study of Clinical Relevance and Role of Alcohol Consumption
Linneberg, A., Fenger, R. V., Husemoen, L., Vidal, C., Vizcaíno, L., & González-Quintela, A. (2010) · International Archives of Allergy and Immunology · doi:10.1159/000301583 · Cited by 18
Production of recombinant allergens in plants
Schmidt, G., Gadermaier, G., Pertl, H., Siegert, M., Oksman-Caldentey, K., Ritala, A., Himly, M., Obermeyer, G., & Ferreira, F. (2008) · Phytochemistry Reviews · doi:10.1007/s11101-008-9099-z · Cited by 18
“In the case of recombinant allergens, correct glycosylation plays an important role and the sugar chains of the recombinant allergen should mimic or be equal to those of the native allergen, as patient’s IgEs might also recognize the glycans of an allergen (Leonard et al. 2005; Altmann 2007).”
Background
Allergy to fungi: Advances in the understanding of fungal allergens
Abel-Fernández, E., & Fernández‐Caldas, E. (2023) · Molecular Immunology · doi:10.1016/j.molimm.2023.09.017 · Cited by 17
Impact of Specific N-Glycan Modifications on the Use of Plant-Produced SARS-CoV-2 Antigens in Serological Assays
Schwestka, J., König-Beihammer, J., Shin, Y., Vavra, U., Kienzl, N. F., Grünwald‐Gruber, C., Maresch, D., Klausberger, M., Laurent, E., Stadler, M., et al. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.747500 · Cited by 19
“Approximately one fifth of patients with allergies develop IgE antibodies against such N-glycans (Altmann, 2007; Holzweber et al., 2013).”
BackgroundSelf-citation

Authors: Altmann, F.
Affiliations: BOKU University (AT)
Corresponding author: Altmann, Friedrich
ORCID: Altmann, Friedrich
Venue: International Archives of Allergy and Immunology
Publisher: S. Karger AG
Published: 2006-10-09
Volume: 142
Issue: 2
Pages: 99-115
ISSN: 1018-2438 (ISSN-L)
1423-0097
DOI: 10.1159/000096114
OpenAlex: W1976454430
Cited by: 393
References: 0
Citations by year: 2026: 11 · 2025: 10 · 2024: 10 · 2023: 10 · 2022: 5 · 2021: 17 · 2020: 20 · 2019: 17 · 2018: 16 · 2017: 23 · 2016: 21 · 2015: 31 · 2014: 25 · 2013: 33 · 2012: 25
FWCI: 1.27
Type: journal article
Language: en
Open access: closed
Licence: www.karger.com/Services/SiteLicenses (vor)
www.karger.com/Services/SiteLicenses (tdm)
Locations: International Archives of Allergy and Immunology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Health Sciences › Medicine › Immunology and Allergy › Allergic Rhinitis and Sensitization
Health Sciences › Medicine › Immunology and Allergy › Food Allergy and Anaphylaxis Research
Keywords: protein glycosylation, allergy, cross-reactive carbohydrate determinants, N-glycans, helminth immunomodulation, pollen allergens, insect venom, food allergens
MeSH terms: Allergens, Animals, Carbohydrate Conformation, Carbohydrates, Glycoproteins, Glycosylation, Humans, Hypersensitivity

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The Role of Protein Glycosylation in Allergy

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