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
Background: Pollen from trees of the order Fagales are important allergen sources in most parts of the world. Clinical, immunochemical, and molecular biology studies indicate that they contain cross-reactive allergens. The major birch pollen allergen, Bet v 1, and birch profilin, Bet v 2, a highly c...
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| Veröffentlicht in: | Journal of allergy and clinical immunology 1998-10, Vol.102 (4), p.579-591 |
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| creator | Niederberger, Verena Pauli, Gabrielle Grönlund c, Hans Fröschl a, Renate Rumpold, Helmut Kraft, Dietrich Valenta, Rudolf Spitzauer, Susanne |
| description | Background: Pollen from trees of the order Fagales are important allergen sources in most parts of the world. Clinical, immunochemical, and molecular biology studies indicate that they contain cross-reactive allergens. The major birch pollen allergen, Bet v 1, and birch profilin, Bet v 2, a highly cross-reactive allergen, have been cloned and expressed in
Escherichia coli. Objective: The purpose of this study was to demonstrate the presence of allergens in Fagales pollens that share IgE epitopes with recombinant Bet v 1 and Bet v 2 and to determine the percentage of birch, alder, hornbeam, hazel, and oak pollen–specific IgE that can be preabsorbed with rBet v 1 and rBet v 2 from 102 sera of different populations of subjects allergic to Fagales tree pollen. Methods: The presence of rBet v 1– and rBet v 2–homologous allergens in tree pollen extracts was investigated by IgE immunoblot inhibition experiments, and the percentage of tree (birch, alder, hornbeam, hazel, and oak) pollen–specific IgE that was bound by a mixture of rBet v 1 and rBet v 2 was determined by RAST-based quantitative IgE inhibition experiments. The clinical significance of IgE antibody cross-reactivity was studied by skin prick testing with rBet v 1, rBet v 2, and Fagales pollen extracts. Results: Natural birch, alder, hornbeam, hazel, and oak pollen contain allergens that share IgE epitopes with rBet v 1 and rBet v 2. A combination of rBet v 1 and rBet v 2 accounted for 82% of tree pollen–specific IgE on average. Most of the tree pollen–specific IgE was directed against rBet v 1. Conclusion: rBet v 1 and rBet v 2 contain most of the Fagales pollen–specific IgE epitopes and may therefore substitute natural tree pollen extracts not only for diagnosis but also for patient-tailored immunotherapy of tree pollen allergy. (J Allergy Clin Immunol 1998;102:579-91.) |
| doi_str_mv | 10.1016/S0091-6749(98)70273-8 |
| format | Article |
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Escherichia coli. Objective: The purpose of this study was to demonstrate the presence of allergens in Fagales pollens that share IgE epitopes with recombinant Bet v 1 and Bet v 2 and to determine the percentage of birch, alder, hornbeam, hazel, and oak pollen–specific IgE that can be preabsorbed with rBet v 1 and rBet v 2 from 102 sera of different populations of subjects allergic to Fagales tree pollen. Methods: The presence of rBet v 1– and rBet v 2–homologous allergens in tree pollen extracts was investigated by IgE immunoblot inhibition experiments, and the percentage of tree (birch, alder, hornbeam, hazel, and oak) pollen–specific IgE that was bound by a mixture of rBet v 1 and rBet v 2 was determined by RAST-based quantitative IgE inhibition experiments. The clinical significance of IgE antibody cross-reactivity was studied by skin prick testing with rBet v 1, rBet v 2, and Fagales pollen extracts. Results: Natural birch, alder, hornbeam, hazel, and oak pollen contain allergens that share IgE epitopes with rBet v 1 and rBet v 2. A combination of rBet v 1 and rBet v 2 accounted for 82% of tree pollen–specific IgE on average. Most of the tree pollen–specific IgE was directed against rBet v 1. Conclusion: rBet v 1 and rBet v 2 contain most of the Fagales pollen–specific IgE epitopes and may therefore substitute natural tree pollen extracts not only for diagnosis but also for patient-tailored immunotherapy of tree pollen allergy. (J Allergy Clin Immunol 1998;102:579-91.)</description><identifier>ISSN: 0091-6749</identifier><identifier>EISSN: 1097-6825</identifier><identifier>DOI: 10.1016/S0091-6749(98)70273-8</identifier><identifier>PMID: 9802365</identifier><identifier>CODEN: JACIBY</identifier><language>eng</language><publisher>New York, NY: Mosby, Inc</publisher><subject>Adult ; Allergens - chemistry ; Allergens - immunology ; Allergic diseases ; Antigens, Plant ; Bet v 1 ; Biological and medical sciences ; Contractile Proteins ; Cross Reactions ; cross-reactivity ; Epitope Mapping ; Female ; General aspects ; Humans ; immunoabsorption ; Immunoglobulin E - immunology ; Immunopathology ; Male ; Medical sciences ; Microfilament Proteins - chemistry ; Microfilament Proteins - immunology ; Middle Aged ; Plant Extracts - chemistry ; Plant Extracts - immunology ; Plant Proteins - chemistry ; Plant Proteins - immunology ; Pollen - chemistry ; Pollen - immunology ; profilin (Bet v 2) ; Profilins ; Radioallergosorbent Test ; Recombinant birch pollen allergens ; Recombinant Proteins - chemistry ; Recombinant Proteins - immunology ; skin prick testing ; Skin Tests ; tree pollen allergy ; Trees</subject><ispartof>Journal of allergy and clinical immunology, 1998-10, Vol.102 (4), p.579-591</ispartof><rights>1998 Mosby, Inc.</rights><rights>1998 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c519t-f83727da5c1acce26e3d0f1106ae6040a7d8b84de144f9e4dcfc25b45d1f50533</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0091674998702738$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2425296$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9802365$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Niederberger, Verena</creatorcontrib><creatorcontrib>Pauli, Gabrielle</creatorcontrib><creatorcontrib>Grönlund c, Hans</creatorcontrib><creatorcontrib>Fröschl a, Renate</creatorcontrib><creatorcontrib>Rumpold, Helmut</creatorcontrib><creatorcontrib>Kraft, Dietrich</creatorcontrib><creatorcontrib>Valenta, Rudolf</creatorcontrib><creatorcontrib>Spitzauer, Susanne</creatorcontrib><title>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</title><title>Journal of allergy and clinical immunology</title><addtitle>J Allergy Clin Immunol</addtitle><description>Background: Pollen from trees of the order Fagales are important allergen sources in most parts of the world. Clinical, immunochemical, and molecular biology studies indicate that they contain cross-reactive allergens. The major birch pollen allergen, Bet v 1, and birch profilin, Bet v 2, a highly cross-reactive allergen, have been cloned and expressed in
Escherichia coli. Objective: The purpose of this study was to demonstrate the presence of allergens in Fagales pollens that share IgE epitopes with recombinant Bet v 1 and Bet v 2 and to determine the percentage of birch, alder, hornbeam, hazel, and oak pollen–specific IgE that can be preabsorbed with rBet v 1 and rBet v 2 from 102 sera of different populations of subjects allergic to Fagales tree pollen. Methods: The presence of rBet v 1– and rBet v 2–homologous allergens in tree pollen extracts was investigated by IgE immunoblot inhibition experiments, and the percentage of tree (birch, alder, hornbeam, hazel, and oak) pollen–specific IgE that was bound by a mixture of rBet v 1 and rBet v 2 was determined by RAST-based quantitative IgE inhibition experiments. The clinical significance of IgE antibody cross-reactivity was studied by skin prick testing with rBet v 1, rBet v 2, and Fagales pollen extracts. Results: Natural birch, alder, hornbeam, hazel, and oak pollen contain allergens that share IgE epitopes with rBet v 1 and rBet v 2. A combination of rBet v 1 and rBet v 2 accounted for 82% of tree pollen–specific IgE on average. Most of the tree pollen–specific IgE was directed against rBet v 1. Conclusion: rBet v 1 and rBet v 2 contain most of the Fagales pollen–specific IgE epitopes and may therefore substitute natural tree pollen extracts not only for diagnosis but also for patient-tailored immunotherapy of tree pollen allergy. (J Allergy Clin Immunol 1998;102:579-91.)</description><subject>Adult</subject><subject>Allergens - chemistry</subject><subject>Allergens - immunology</subject><subject>Allergic diseases</subject><subject>Antigens, Plant</subject><subject>Bet v 1</subject><subject>Biological and medical sciences</subject><subject>Contractile Proteins</subject><subject>Cross Reactions</subject><subject>cross-reactivity</subject><subject>Epitope Mapping</subject><subject>Female</subject><subject>General aspects</subject><subject>Humans</subject><subject>immunoabsorption</subject><subject>Immunoglobulin E - immunology</subject><subject>Immunopathology</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Microfilament Proteins - chemistry</subject><subject>Microfilament Proteins - immunology</subject><subject>Middle Aged</subject><subject>Plant Extracts - chemistry</subject><subject>Plant Extracts - immunology</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - immunology</subject><subject>Pollen - chemistry</subject><subject>Pollen - immunology</subject><subject>profilin (Bet v 2)</subject><subject>Profilins</subject><subject>Radioallergosorbent Test</subject><subject>Recombinant birch pollen allergens</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - immunology</subject><subject>skin prick testing</subject><subject>Skin Tests</subject><subject>tree pollen allergy</subject><subject>Trees</subject><issn>0091-6749</issn><issn>1097-6825</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkttu1DAQhiMEKkvhESrNBUKttAE7iXPgBpWqQKVKSByuLccedw2JndrOovKwPAve3Whve2N7NN_888szWXZGyVtKaP3uOyEdzeum6s679qIhRVPm7ZNsRUnX5HVbsKfZ6og8z16E8IukuGy7k-yka0lR1myV_fuG0o29scJG6I2XG5jcMKAFkU5_hzbAuf-IEbZAQVgFS1BcgHQ2CmNhdCGC0xA3CDd314CTiW7CAJPHgEk3MXvpdRJV6Newcd72KMb0En9xWO-Fnfi99H4Pl3A_J0cmimi2B1VjN6Y30TgLIc7qAf6YuIGAXoD2bgRltEa_aze5aR7Ejgwvs2daDAFfLfdp9vPT9Y-rL_nt1883V5e3uWS0i7luy6ZolGCSCimxqLFURFNKaoE1qYhoVNu3lUJaVbrDSkktC9ZXTFHNCCvL0-zNQXfy7n7GEPlogsRhEBbdHHhDCG1Y0T0K0uSjYyVLIDuA0rsQPGo-eTMK_8Ap4bsF4PsF4Lvp8q7l-wXgbao7WxrM_YjqWLVMPOVfL3kRpBi0F1aacMSKqkg264R9OGCYfm1r0PMgDVqJyniUkStnHjHyH8QGz-U</recordid><startdate>19981001</startdate><enddate>19981001</enddate><creator>Niederberger, Verena</creator><creator>Pauli, Gabrielle</creator><creator>Grönlund c, Hans</creator><creator>Fröschl a, Renate</creator><creator>Rumpold, Helmut</creator><creator>Kraft, Dietrich</creator><creator>Valenta, Rudolf</creator><creator>Spitzauer, Susanne</creator><general>Mosby, Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19981001</creationdate><title>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</title><author>Niederberger, Verena ; Pauli, Gabrielle ; Grönlund c, Hans ; Fröschl a, Renate ; Rumpold, Helmut ; Kraft, Dietrich ; Valenta, Rudolf ; Spitzauer, Susanne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c519t-f83727da5c1acce26e3d0f1106ae6040a7d8b84de144f9e4dcfc25b45d1f50533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Adult</topic><topic>Allergens - chemistry</topic><topic>Allergens - immunology</topic><topic>Allergic diseases</topic><topic>Antigens, Plant</topic><topic>Bet v 1</topic><topic>Biological and medical sciences</topic><topic>Contractile Proteins</topic><topic>Cross Reactions</topic><topic>cross-reactivity</topic><topic>Epitope Mapping</topic><topic>Female</topic><topic>General aspects</topic><topic>Humans</topic><topic>immunoabsorption</topic><topic>Immunoglobulin E - immunology</topic><topic>Immunopathology</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Microfilament Proteins - chemistry</topic><topic>Microfilament Proteins - immunology</topic><topic>Middle Aged</topic><topic>Plant Extracts - chemistry</topic><topic>Plant Extracts - immunology</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - immunology</topic><topic>Pollen - chemistry</topic><topic>Pollen - immunology</topic><topic>profilin (Bet v 2)</topic><topic>Profilins</topic><topic>Radioallergosorbent Test</topic><topic>Recombinant birch pollen allergens</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - immunology</topic><topic>skin prick testing</topic><topic>Skin Tests</topic><topic>tree pollen allergy</topic><topic>Trees</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Niederberger, Verena</creatorcontrib><creatorcontrib>Pauli, Gabrielle</creatorcontrib><creatorcontrib>Grönlund c, Hans</creatorcontrib><creatorcontrib>Fröschl a, Renate</creatorcontrib><creatorcontrib>Rumpold, Helmut</creatorcontrib><creatorcontrib>Kraft, Dietrich</creatorcontrib><creatorcontrib>Valenta, Rudolf</creatorcontrib><creatorcontrib>Spitzauer, Susanne</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of allergy and clinical immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Niederberger, Verena</au><au>Pauli, Gabrielle</au><au>Grönlund c, Hans</au><au>Fröschl a, Renate</au><au>Rumpold, Helmut</au><au>Kraft, Dietrich</au><au>Valenta, Rudolf</au><au>Spitzauer, Susanne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>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</atitle><jtitle>Journal of allergy and clinical immunology</jtitle><addtitle>J Allergy Clin Immunol</addtitle><date>1998-10-01</date><risdate>1998</risdate><volume>102</volume><issue>4</issue><spage>579</spage><epage>591</epage><pages>579-591</pages><issn>0091-6749</issn><eissn>1097-6825</eissn><coden>JACIBY</coden><abstract>Background: Pollen from trees of the order Fagales are important allergen sources in most parts of the world. Clinical, immunochemical, and molecular biology studies indicate that they contain cross-reactive allergens. The major birch pollen allergen, Bet v 1, and birch profilin, Bet v 2, a highly cross-reactive allergen, have been cloned and expressed in
Escherichia coli. Objective: The purpose of this study was to demonstrate the presence of allergens in Fagales pollens that share IgE epitopes with recombinant Bet v 1 and Bet v 2 and to determine the percentage of birch, alder, hornbeam, hazel, and oak pollen–specific IgE that can be preabsorbed with rBet v 1 and rBet v 2 from 102 sera of different populations of subjects allergic to Fagales tree pollen. Methods: The presence of rBet v 1– and rBet v 2–homologous allergens in tree pollen extracts was investigated by IgE immunoblot inhibition experiments, and the percentage of tree (birch, alder, hornbeam, hazel, and oak) pollen–specific IgE that was bound by a mixture of rBet v 1 and rBet v 2 was determined by RAST-based quantitative IgE inhibition experiments. The clinical significance of IgE antibody cross-reactivity was studied by skin prick testing with rBet v 1, rBet v 2, and Fagales pollen extracts. Results: Natural birch, alder, hornbeam, hazel, and oak pollen contain allergens that share IgE epitopes with rBet v 1 and rBet v 2. A combination of rBet v 1 and rBet v 2 accounted for 82% of tree pollen–specific IgE on average. Most of the tree pollen–specific IgE was directed against rBet v 1. Conclusion: rBet v 1 and rBet v 2 contain most of the Fagales pollen–specific IgE epitopes and may therefore substitute natural tree pollen extracts not only for diagnosis but also for patient-tailored immunotherapy of tree pollen allergy. (J Allergy Clin Immunol 1998;102:579-91.)</abstract><cop>New York, NY</cop><pub>Mosby, Inc</pub><pmid>9802365</pmid><doi>10.1016/S0091-6749(98)70273-8</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adult Allergens - chemistry Allergens - immunology Allergic diseases Antigens, Plant Bet v 1 Biological and medical sciences Contractile Proteins Cross Reactions cross-reactivity Epitope Mapping Female General aspects Humans immunoabsorption Immunoglobulin E - immunology Immunopathology Male Medical sciences Microfilament Proteins - chemistry Microfilament Proteins - immunology Middle Aged Plant Extracts - chemistry Plant Extracts - immunology Plant Proteins - chemistry Plant Proteins - immunology Pollen - chemistry Pollen - immunology profilin (Bet v 2) Profilins Radioallergosorbent Test Recombinant birch pollen allergens Recombinant Proteins - chemistry Recombinant Proteins - immunology skin prick testing Skin Tests tree pollen allergy Trees |
| title | 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 |
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