Hypoallergenic derivatives of the major birch pollen allergen Bet v 1 obtained by rational sequence reassembly
Background At least 100 million patients suffer from birch pollen allergy. Objective Rational design of recombinant derivatives of the major birch pollen allergen, Bet v 1, characterized by reduced IgE reactivity, preservation of sequences relevant for the induction of allergen-specific blocking IgG...
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| creator | Campana, Raffaela, PhD Vrtala, Susanne, PhD Maderegger, Bernhard, PhD Jertschin, Peter, PhD Stegfellner, Gottfried, PhD Swoboda, Ines, PhD Focke-Tejkl, Margarete, PhD Blatt, Katharina Gieras, Anna, MSc Zafred, Domen, BSc Neubauer, Angela, PhD Valent, Peter, MD Keller, Walter, PhD Spitzauer, Susanne, MD Valenta, Rudolf, MD |
| description | Background At least 100 million patients suffer from birch pollen allergy. Objective Rational design of recombinant derivatives of the major birch pollen allergen, Bet v 1, characterized by reduced IgE reactivity, preservation of sequences relevant for the induction of allergen-specific blocking IgG, and maintenance of T-cell epitopes for immunotherapy of birch pollen allergy. Methods Three recombinant mosaic proteins derived from Bet v 1 were generated by reassembly of codon-optimized genes coding for Bet v 1 fragments containing the elements for the induction of allergen-specific blocking IgG antibodies and the major T-cell epitopes. The proteins were expressed in Escherichia coli as recombinant mosaic molecules and compared with the Bet v 1 wild-type protein by chemical and structural methods, regarding IgE-binding and IgG-binding capacity, in basophil activation assays and tested for the in vivo induction of IgG responses. Results Three recombinant Bet v 1 (rBet v 1) mosaic proteins with strongly reduced IgE reactivity and allergenic activity were expressed and purified. Immunization with the recombinant hypoallergens induced IgG antibodies that inhibited IgE reactivity of patients with allergy to Bet v 1 comparable to those induced with the rBet v 1 wild-type allergen. Conclusion We report the generation and preclinical characterization of 3 hypoallergenic rBet v 1 derivatives with suitable properties for immunotherapy of birch pollen allergy. |
| doi_str_mv | 10.1016/j.jaci.2010.05.023 |
| format | Article |
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Objective Rational design of recombinant derivatives of the major birch pollen allergen, Bet v 1, characterized by reduced IgE reactivity, preservation of sequences relevant for the induction of allergen-specific blocking IgG, and maintenance of T-cell epitopes for immunotherapy of birch pollen allergy. Methods Three recombinant mosaic proteins derived from Bet v 1 were generated by reassembly of codon-optimized genes coding for Bet v 1 fragments containing the elements for the induction of allergen-specific blocking IgG antibodies and the major T-cell epitopes. The proteins were expressed in Escherichia coli as recombinant mosaic molecules and compared with the Bet v 1 wild-type protein by chemical and structural methods, regarding IgE-binding and IgG-binding capacity, in basophil activation assays and tested for the in vivo induction of IgG responses. Results Three recombinant Bet v 1 (rBet v 1) mosaic proteins with strongly reduced IgE reactivity and allergenic activity were expressed and purified. Immunization with the recombinant hypoallergens induced IgG antibodies that inhibited IgE reactivity of patients with allergy to Bet v 1 comparable to those induced with the rBet v 1 wild-type allergen. Conclusion We report the generation and preclinical characterization of 3 hypoallergenic rBet v 1 derivatives with suitable properties for immunotherapy of birch pollen allergy.</description><identifier>ISSN: 0091-6749</identifier><identifier>EISSN: 1097-6825</identifier><identifier>DOI: 10.1016/j.jaci.2010.05.023</identifier><identifier>PMID: 20638112</identifier><identifier>CODEN: JACIBY</identifier><language>eng</language><publisher>New York, NY: Mosby, Inc</publisher><subject>Allergens ; Allergies ; Allergy and Immunology ; Amino acids ; Animals ; Antigens, Plant - chemistry ; Antigens, Plant - immunology ; Betula - immunology ; Biological and medical sciences ; Birch pollen allergy ; Derivatives ; Enzyme-Linked Immunosorbent Assay ; Epitopes, T-Lymphocyte - chemistry ; Epitopes, T-Lymphocyte - immunology ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; Immunopathology ; immunotherapy ; Immunotherapy - methods ; Medical sciences ; Peptides ; Plant Proteins - chemical synthesis ; Plant Proteins - chemistry ; Plant Proteins - immunology ; Pollen ; Pollen - immunology ; Proteins ; Rabbits ; rBet v 1 ; recombinant hypoallergenic derivative molecules ; Recombinant Proteins - chemical synthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - immunology ; Rhinitis, Allergic, Seasonal - immunology ; Sarcoidosis. Granulomatous diseases of unproved etiology. Connective tissue diseases. Elastic tissue diseases. Vasculitis</subject><ispartof>Journal of allergy and clinical immunology, 2010-11, Vol.126 (5), p.1024-1031.e8</ispartof><rights>American Academy of Allergy, Asthma & Immunology</rights><rights>2010 American Academy of Allergy, Asthma & Immunology</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2010 American Academy of Allergy, Asthma & Immunology. Published by Mosby, Inc. All rights reserved.</rights><rights>Copyright Elsevier Limited Nov 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c500t-20c4d59a752d39562b51654df3e1506d09481c12caf89419444ceae23c34c8bc3</citedby><cites>FETCH-LOGICAL-c500t-20c4d59a752d39562b51654df3e1506d09481c12caf89419444ceae23c34c8bc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0091674910008286$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23530296$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20638112$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Campana, Raffaela, PhD</creatorcontrib><creatorcontrib>Vrtala, Susanne, PhD</creatorcontrib><creatorcontrib>Maderegger, Bernhard, PhD</creatorcontrib><creatorcontrib>Jertschin, Peter, PhD</creatorcontrib><creatorcontrib>Stegfellner, Gottfried, PhD</creatorcontrib><creatorcontrib>Swoboda, Ines, PhD</creatorcontrib><creatorcontrib>Focke-Tejkl, Margarete, PhD</creatorcontrib><creatorcontrib>Blatt, Katharina</creatorcontrib><creatorcontrib>Gieras, Anna, MSc</creatorcontrib><creatorcontrib>Zafred, Domen, BSc</creatorcontrib><creatorcontrib>Neubauer, Angela, PhD</creatorcontrib><creatorcontrib>Valent, Peter, MD</creatorcontrib><creatorcontrib>Keller, Walter, PhD</creatorcontrib><creatorcontrib>Spitzauer, Susanne, MD</creatorcontrib><creatorcontrib>Valenta, Rudolf, MD</creatorcontrib><title>Hypoallergenic derivatives of the major birch pollen allergen Bet v 1 obtained by rational sequence reassembly</title><title>Journal of allergy and clinical immunology</title><addtitle>J Allergy Clin Immunol</addtitle><description>Background At least 100 million patients suffer from birch pollen allergy. Objective Rational design of recombinant derivatives of the major birch pollen allergen, Bet v 1, characterized by reduced IgE reactivity, preservation of sequences relevant for the induction of allergen-specific blocking IgG, and maintenance of T-cell epitopes for immunotherapy of birch pollen allergy. Methods Three recombinant mosaic proteins derived from Bet v 1 were generated by reassembly of codon-optimized genes coding for Bet v 1 fragments containing the elements for the induction of allergen-specific blocking IgG antibodies and the major T-cell epitopes. The proteins were expressed in Escherichia coli as recombinant mosaic molecules and compared with the Bet v 1 wild-type protein by chemical and structural methods, regarding IgE-binding and IgG-binding capacity, in basophil activation assays and tested for the in vivo induction of IgG responses. Results Three recombinant Bet v 1 (rBet v 1) mosaic proteins with strongly reduced IgE reactivity and allergenic activity were expressed and purified. Immunization with the recombinant hypoallergens induced IgG antibodies that inhibited IgE reactivity of patients with allergy to Bet v 1 comparable to those induced with the rBet v 1 wild-type allergen. Conclusion We report the generation and preclinical characterization of 3 hypoallergenic rBet v 1 derivatives with suitable properties for immunotherapy of birch pollen allergy.</description><subject>Allergens</subject><subject>Allergies</subject><subject>Allergy and Immunology</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antigens, Plant - chemistry</subject><subject>Antigens, Plant - immunology</subject><subject>Betula - immunology</subject><subject>Biological and medical sciences</subject><subject>Birch pollen allergy</subject><subject>Derivatives</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Epitopes, T-Lymphocyte - chemistry</subject><subject>Epitopes, T-Lymphocyte - immunology</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Humans</subject><subject>Immunopathology</subject><subject>immunotherapy</subject><subject>Immunotherapy - methods</subject><subject>Medical sciences</subject><subject>Peptides</subject><subject>Plant Proteins - chemical synthesis</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - immunology</subject><subject>Pollen</subject><subject>Pollen - immunology</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>rBet v 1</subject><subject>recombinant hypoallergenic derivative molecules</subject><subject>Recombinant Proteins - chemical synthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - immunology</subject><subject>Rhinitis, Allergic, Seasonal - immunology</subject><subject>Sarcoidosis. Granulomatous diseases of unproved etiology. Connective tissue diseases. Elastic tissue diseases. Vasculitis</subject><issn>0091-6749</issn><issn>1097-6825</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkl-L1DAUxYMo7rj6BXyQgIhPHfO_DciCLuoKCz6ozyFNb93UtBmTzkC_vakz68I-6FNI-J3LuTkHoeeUbCmh6s2wHazzW0bKA5FbwvgDtKFE15VqmHyINoRoWqla6DP0JOeBlDtv9GN0xojiDaVsg6arZRdtCJB-wOQd7iD5g539ATKOPZ5vAI92iAm3PrkbvIsFnfCtAL-HGR8wxbGdrZ-gw-2CU5HHyQac4dceJgc4gc0ZxjYsT9Gj3oYMz07nOfr-8cO3y6vq-sunz5fvrisnCZkrRpzopLa1ZB3XUrFWUiVF13OgkqiOaNFQR5mzfaMF1UIIBxYYd1y4pnX8HL0-zt2lWEzk2Yw-OwjBThD32TSSi1qQuv4vWSumaqUVK-TLe-QQ96ksmk0xJRrGxB-KHSmXYs4JerNLfrRpMZSYNTYzmDU2s8ZmiDQltiJ6cRq9b0fo_kpucyrAqxNgs7OhT3ZyPt9xXHLCtCrc2yMH5XMPHpLJzq8ZdD6Bm00X_b99XNyTu-BLLWz4CQvku31NZoaYr2vB1n7RUq2GNYr_Bg7OyW4</recordid><startdate>20101101</startdate><enddate>20101101</enddate><creator>Campana, Raffaela, PhD</creator><creator>Vrtala, Susanne, PhD</creator><creator>Maderegger, Bernhard, PhD</creator><creator>Jertschin, Peter, PhD</creator><creator>Stegfellner, Gottfried, PhD</creator><creator>Swoboda, Ines, PhD</creator><creator>Focke-Tejkl, Margarete, PhD</creator><creator>Blatt, Katharina</creator><creator>Gieras, Anna, MSc</creator><creator>Zafred, Domen, BSc</creator><creator>Neubauer, Angela, PhD</creator><creator>Valent, Peter, MD</creator><creator>Keller, Walter, PhD</creator><creator>Spitzauer, Susanne, MD</creator><creator>Valenta, Rudolf, MD</creator><general>Mosby, Inc</general><general>Elsevier</general><general>Elsevier Limited</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>7SS</scope><scope>7T5</scope><scope>H94</scope><scope>K9.</scope><scope>NAPCQ</scope><scope>7X8</scope><scope>7U7</scope><scope>C1K</scope></search><sort><creationdate>20101101</creationdate><title>Hypoallergenic derivatives of the major birch pollen allergen Bet v 1 obtained by rational sequence reassembly</title><author>Campana, Raffaela, PhD ; Vrtala, Susanne, PhD ; Maderegger, Bernhard, PhD ; Jertschin, Peter, PhD ; Stegfellner, Gottfried, PhD ; Swoboda, Ines, PhD ; Focke-Tejkl, Margarete, PhD ; Blatt, Katharina ; Gieras, Anna, MSc ; Zafred, Domen, BSc ; Neubauer, Angela, PhD ; Valent, Peter, MD ; Keller, Walter, PhD ; Spitzauer, Susanne, MD ; Valenta, Rudolf, MD</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c500t-20c4d59a752d39562b51654df3e1506d09481c12caf89419444ceae23c34c8bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Allergens</topic><topic>Allergies</topic><topic>Allergy and Immunology</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Antigens, Plant - chemistry</topic><topic>Antigens, Plant - immunology</topic><topic>Betula - immunology</topic><topic>Biological and medical sciences</topic><topic>Birch pollen allergy</topic><topic>Derivatives</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Epitopes, T-Lymphocyte - chemistry</topic><topic>Epitopes, T-Lymphocyte - immunology</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Humans</topic><topic>Immunopathology</topic><topic>immunotherapy</topic><topic>Immunotherapy - methods</topic><topic>Medical sciences</topic><topic>Peptides</topic><topic>Plant Proteins - chemical synthesis</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - immunology</topic><topic>Pollen</topic><topic>Pollen - immunology</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>rBet v 1</topic><topic>recombinant hypoallergenic derivative molecules</topic><topic>Recombinant Proteins - chemical synthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - immunology</topic><topic>Rhinitis, Allergic, Seasonal - immunology</topic><topic>Sarcoidosis. Granulomatous diseases of unproved etiology. Connective tissue diseases. Elastic tissue diseases. Vasculitis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Campana, Raffaela, PhD</creatorcontrib><creatorcontrib>Vrtala, Susanne, PhD</creatorcontrib><creatorcontrib>Maderegger, Bernhard, PhD</creatorcontrib><creatorcontrib>Jertschin, Peter, PhD</creatorcontrib><creatorcontrib>Stegfellner, Gottfried, PhD</creatorcontrib><creatorcontrib>Swoboda, Ines, PhD</creatorcontrib><creatorcontrib>Focke-Tejkl, Margarete, PhD</creatorcontrib><creatorcontrib>Blatt, Katharina</creatorcontrib><creatorcontrib>Gieras, Anna, MSc</creatorcontrib><creatorcontrib>Zafred, Domen, BSc</creatorcontrib><creatorcontrib>Neubauer, Angela, PhD</creatorcontrib><creatorcontrib>Valent, Peter, MD</creatorcontrib><creatorcontrib>Keller, Walter, PhD</creatorcontrib><creatorcontrib>Spitzauer, Susanne, MD</creatorcontrib><creatorcontrib>Valenta, Rudolf, MD</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>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Premium</collection><collection>MEDLINE - Academic</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Journal of allergy and clinical immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Campana, Raffaela, PhD</au><au>Vrtala, Susanne, PhD</au><au>Maderegger, Bernhard, PhD</au><au>Jertschin, Peter, PhD</au><au>Stegfellner, Gottfried, PhD</au><au>Swoboda, Ines, PhD</au><au>Focke-Tejkl, Margarete, PhD</au><au>Blatt, Katharina</au><au>Gieras, Anna, MSc</au><au>Zafred, Domen, BSc</au><au>Neubauer, Angela, PhD</au><au>Valent, Peter, MD</au><au>Keller, Walter, PhD</au><au>Spitzauer, Susanne, MD</au><au>Valenta, Rudolf, MD</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hypoallergenic derivatives of the major birch pollen allergen Bet v 1 obtained by rational sequence reassembly</atitle><jtitle>Journal of allergy and clinical immunology</jtitle><addtitle>J Allergy Clin Immunol</addtitle><date>2010-11-01</date><risdate>2010</risdate><volume>126</volume><issue>5</issue><spage>1024</spage><epage>1031.e8</epage><pages>1024-1031.e8</pages><issn>0091-6749</issn><eissn>1097-6825</eissn><coden>JACIBY</coden><abstract>Background At least 100 million patients suffer from birch pollen allergy. Objective Rational design of recombinant derivatives of the major birch pollen allergen, Bet v 1, characterized by reduced IgE reactivity, preservation of sequences relevant for the induction of allergen-specific blocking IgG, and maintenance of T-cell epitopes for immunotherapy of birch pollen allergy. Methods Three recombinant mosaic proteins derived from Bet v 1 were generated by reassembly of codon-optimized genes coding for Bet v 1 fragments containing the elements for the induction of allergen-specific blocking IgG antibodies and the major T-cell epitopes. The proteins were expressed in Escherichia coli as recombinant mosaic molecules and compared with the Bet v 1 wild-type protein by chemical and structural methods, regarding IgE-binding and IgG-binding capacity, in basophil activation assays and tested for the in vivo induction of IgG responses. Results Three recombinant Bet v 1 (rBet v 1) mosaic proteins with strongly reduced IgE reactivity and allergenic activity were expressed and purified. Immunization with the recombinant hypoallergens induced IgG antibodies that inhibited IgE reactivity of patients with allergy to Bet v 1 comparable to those induced with the rBet v 1 wild-type allergen. Conclusion We report the generation and preclinical characterization of 3 hypoallergenic rBet v 1 derivatives with suitable properties for immunotherapy of birch pollen allergy.</abstract><cop>New York, NY</cop><pub>Mosby, Inc</pub><pmid>20638112</pmid><doi>10.1016/j.jaci.2010.05.023</doi><tpages>8</tpages></addata></record> |
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| subjects | Allergens Allergies Allergy and Immunology Amino acids Animals Antigens, Plant - chemistry Antigens, Plant - immunology Betula - immunology Biological and medical sciences Birch pollen allergy Derivatives Enzyme-Linked Immunosorbent Assay Epitopes, T-Lymphocyte - chemistry Epitopes, T-Lymphocyte - immunology Escherichia coli Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immunopathology immunotherapy Immunotherapy - methods Medical sciences Peptides Plant Proteins - chemical synthesis Plant Proteins - chemistry Plant Proteins - immunology Pollen Pollen - immunology Proteins Rabbits rBet v 1 recombinant hypoallergenic derivative molecules Recombinant Proteins - chemical synthesis Recombinant Proteins - chemistry Recombinant Proteins - immunology Rhinitis, Allergic, Seasonal - immunology Sarcoidosis. Granulomatous diseases of unproved etiology. Connective tissue diseases. Elastic tissue diseases. Vasculitis |
| title | Hypoallergenic derivatives of the major birch pollen allergen Bet v 1 obtained by rational sequence reassembly |
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