Characterization of Api g 1.0201, a New Member of the Api g 1 Family of Celery Allergens
Background: The association of pollinosis with allergy to plant foods occurs in up to 70% of tree pollen-allergic patients. In recent years, some of the relevant cross-reacting proteins have been characterized at the molecular and immunological level. Api g 1 has been identified as the celery homolo...
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description | Background: The association of pollinosis with allergy to plant foods occurs in up to 70% of tree pollen-allergic patients. In recent years, some of the relevant cross-reacting proteins have been characterized at the molecular and immunological level. Api g 1 has been identified as the celery homologue of the major birch pollen allergen, Bet v 1. Although a number of Bet v 1 isoforms have been characterized from birch pollen, little is known about isoforms of food allergens and their allergenic features. Methods: Api g 1.0201, an isoform of Api g 1, was isolated from a cDNA library, cloned and sequenced. The cDNA was expressed in Escherichia coli and the purified recombinant protein was tested in immunoblots. Results: Api g 1.0201 displays 72% sequence similarity to the previously identified Api g 1.0101 and consists of 159 amino acid residues. The sequence of Api g 1.0201 has five additional amino acid residues at the carboxy-terminus as compared to Api g 1.0101. Purified recombinant Api g 1.0201 is recognized by IgE from the sera of celery-allergic patients, as well as by the murine monoclonal anti-Bet v 1 antibody. In general, this isoform displays a weaker IgE-binding capacity than Api g 1.0101, as concluded from immunoblotting experiments. Results from inhibition assays revealed that IgE-binding to Api g 1.0201 is only slightly reduced by preincubation with either purified recombinant Api g 1.0101 or purified recombinant Bet v 1a. Total inhibition was only achieved when using purified natural Bet v 1. Conclusions: At present, little is known about the IgE-binding capacity of isoforms of Bet v 1 homologues of food allergens. Identification and characterization of such isoforms may help to contribute to a better understanding of food allergy and the observed cross-reactivity to pollen allergy. |
doi_str_mv | 10.1159/000024367 |
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In recent years, some of the relevant cross-reacting proteins have been characterized at the molecular and immunological level. Api g 1 has been identified as the celery homologue of the major birch pollen allergen, Bet v 1. Although a number of Bet v 1 isoforms have been characterized from birch pollen, little is known about isoforms of food allergens and their allergenic features. Methods: Api g 1.0201, an isoform of Api g 1, was isolated from a cDNA library, cloned and sequenced. The cDNA was expressed in Escherichia coli and the purified recombinant protein was tested in immunoblots. Results: Api g 1.0201 displays 72% sequence similarity to the previously identified Api g 1.0101 and consists of 159 amino acid residues. The sequence of Api g 1.0201 has five additional amino acid residues at the carboxy-terminus as compared to Api g 1.0101. Purified recombinant Api g 1.0201 is recognized by IgE from the sera of celery-allergic patients, as well as by the murine monoclonal anti-Bet v 1 antibody. In general, this isoform displays a weaker IgE-binding capacity than Api g 1.0101, as concluded from immunoblotting experiments. Results from inhibition assays revealed that IgE-binding to Api g 1.0201 is only slightly reduced by preincubation with either purified recombinant Api g 1.0101 or purified recombinant Bet v 1a. Total inhibition was only achieved when using purified natural Bet v 1. Conclusions: At present, little is known about the IgE-binding capacity of isoforms of Bet v 1 homologues of food allergens. Identification and characterization of such isoforms may help to contribute to a better understanding of food allergy and the observed cross-reactivity to pollen allergy.</description><identifier>ISSN: 1018-2438</identifier><identifier>EISSN: 1423-0097</identifier><identifier>DOI: 10.1159/000024367</identifier><identifier>PMID: 10878490</identifier><language>eng</language><publisher>Basel, Switzerland: Karger</publisher><subject>Allergens - chemistry ; Allergens - genetics ; Allergens - immunology ; Allergic diseases ; Amino Acid Sequence ; Antibodies, Monoclonal - immunology ; Antigens, Plant ; Api g 1 antigen ; Apiaceae - chemistry ; Apiaceae - genetics ; Apiaceae - immunology ; Apium graveolens dulce ; Base Sequence ; Biological and medical sciences ; Cloning, Molecular ; DNA, Complementary - analysis ; DNA, Complementary - genetics ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Food Hypersensitivity - blood ; Food Hypersensitivity - immunology ; Humans ; Immunoblotting ; Immunoglobulin E - immunology ; Immunoglobulin E - metabolism ; Immunoglobulin G - immunology ; Immunopathology ; Medical sciences ; Models, Molecular ; Molecular Sequence Data ; Original Paper ; Other localizations ; Plant Proteins - chemistry ; Plant Proteins - genetics ; Plant Proteins - immunology ; Protein Isoforms ; Sequence Homology, Amino Acid</subject><ispartof>International archives of allergy and immunology, 2000-06, Vol.122 (2), p.115-123</ispartof><rights>2000 S. Karger AG, Basel</rights><rights>2000 INIST-CNRS</rights><rights>Copyright 2000 S. Karger AG, Basel.</rights><rights>Copyright (c) 2000 S. Karger AG, Basel</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-18f97bdc1c81fb694b2c501b6553eef8b35694bfdbf16498a5ab889060fce1fe3</citedby><cites>FETCH-LOGICAL-c415t-18f97bdc1c81fb694b2c501b6553eef8b35694bfdbf16498a5ab889060fce1fe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,2423,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1410256$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10878490$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hoffmann-Sommergruber, Karin</creatorcontrib><creatorcontrib>Ferris, Rosemary</creatorcontrib><creatorcontrib>Pec, Martina</creatorcontrib><creatorcontrib>Radauer, Christian</creatorcontrib><creatorcontrib>O’Riordain, Gabriel</creatorcontrib><creatorcontrib>Laimer da Camara Machado, Margit</creatorcontrib><creatorcontrib>Scheiner, Otto</creatorcontrib><creatorcontrib>Breiteneder, Heimo</creatorcontrib><title>Characterization of Api g 1.0201, a New Member of the Api g 1 Family of Celery Allergens</title><title>International archives of allergy and immunology</title><addtitle>Int Arch Allergy Immunol</addtitle><description>Background: The association of pollinosis with allergy to plant foods occurs in up to 70% of tree pollen-allergic patients. In recent years, some of the relevant cross-reacting proteins have been characterized at the molecular and immunological level. Api g 1 has been identified as the celery homologue of the major birch pollen allergen, Bet v 1. Although a number of Bet v 1 isoforms have been characterized from birch pollen, little is known about isoforms of food allergens and their allergenic features. Methods: Api g 1.0201, an isoform of Api g 1, was isolated from a cDNA library, cloned and sequenced. The cDNA was expressed in Escherichia coli and the purified recombinant protein was tested in immunoblots. Results: Api g 1.0201 displays 72% sequence similarity to the previously identified Api g 1.0101 and consists of 159 amino acid residues. The sequence of Api g 1.0201 has five additional amino acid residues at the carboxy-terminus as compared to Api g 1.0101. Purified recombinant Api g 1.0201 is recognized by IgE from the sera of celery-allergic patients, as well as by the murine monoclonal anti-Bet v 1 antibody. In general, this isoform displays a weaker IgE-binding capacity than Api g 1.0101, as concluded from immunoblotting experiments. Results from inhibition assays revealed that IgE-binding to Api g 1.0201 is only slightly reduced by preincubation with either purified recombinant Api g 1.0101 or purified recombinant Bet v 1a. Total inhibition was only achieved when using purified natural Bet v 1. Conclusions: At present, little is known about the IgE-binding capacity of isoforms of Bet v 1 homologues of food allergens. Identification and characterization of such isoforms may help to contribute to a better understanding of food allergy and the observed cross-reactivity to pollen allergy.</description><subject>Allergens - chemistry</subject><subject>Allergens - genetics</subject><subject>Allergens - immunology</subject><subject>Allergic diseases</subject><subject>Amino Acid Sequence</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antigens, Plant</subject><subject>Api g 1 antigen</subject><subject>Apiaceae - chemistry</subject><subject>Apiaceae - genetics</subject><subject>Apiaceae - immunology</subject><subject>Apium graveolens dulce</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - analysis</subject><subject>DNA, Complementary - genetics</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Food Hypersensitivity - blood</subject><subject>Food Hypersensitivity - immunology</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Immunoglobulin E - immunology</subject><subject>Immunoglobulin E - metabolism</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunopathology</subject><subject>Medical sciences</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Original Paper</subject><subject>Other localizations</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - immunology</subject><subject>Protein Isoforms</subject><subject>Sequence Homology, Amino Acid</subject><issn>1018-2438</issn><issn>1423-0097</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0d1rFDEQAPAgFvuhDz4LEooIQrfOJJvd7ONyWC1UfVHwbUlyk3brflyTPeT615v1rq0UwbxMmPmRITOMvUQ4RVTVe0hH5LIon7ADzIXMAKryaboD6iwV9D47jPEaIGFdPGP7CLrUeQUH7MfiygTjJgrtrZnaceCj5_Wq5ZccT0EAnnDDv9Av_pl6S2GuTld0J_iZ6dtuM2cX1FHY8LpL4ZKG-JztedNFerGLR-z72Ydvi0_ZxdeP54v6InM5qilD7avSLh06jd4WVW6FU4C2UEoSeW2lmpN-aT0WeaWNMlbrCgrwjtCTPGJvt--uwnizpjg1fRsddZ0ZaFzHpkQhKynkfyGWBWKaY4LHj-D1uA5D-kQjBGqlBBQJvdsiF8YYA_lmFdrehE2D0MxLae6Xkuzr3YNr29PyL7ndQgJvdsBEZzofzODa-OByBKHmnq-27KdJIw739bsux_-sntf1H9Csll7-BtAoo1g</recordid><startdate>20000601</startdate><enddate>20000601</enddate><creator>Hoffmann-Sommergruber, Karin</creator><creator>Ferris, Rosemary</creator><creator>Pec, Martina</creator><creator>Radauer, Christian</creator><creator>O’Riordain, Gabriel</creator><creator>Laimer da Camara Machado, Margit</creator><creator>Scheiner, Otto</creator><creator>Breiteneder, Heimo</creator><general>Karger</general><general>S. 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chemistry</topic><topic>Allergens - genetics</topic><topic>Allergens - immunology</topic><topic>Allergic diseases</topic><topic>Amino Acid Sequence</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antigens, Plant</topic><topic>Api g 1 antigen</topic><topic>Apiaceae - chemistry</topic><topic>Apiaceae - genetics</topic><topic>Apiaceae - immunology</topic><topic>Apium graveolens dulce</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - analysis</topic><topic>DNA, Complementary - genetics</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Food Hypersensitivity - blood</topic><topic>Food Hypersensitivity - immunology</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Immunoglobulin E - immunology</topic><topic>Immunoglobulin E - metabolism</topic><topic>Immunoglobulin G - immunology</topic><topic>Immunopathology</topic><topic>Medical sciences</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Original Paper</topic><topic>Other localizations</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - immunology</topic><topic>Protein Isoforms</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hoffmann-Sommergruber, Karin</creatorcontrib><creatorcontrib>Ferris, Rosemary</creatorcontrib><creatorcontrib>Pec, Martina</creatorcontrib><creatorcontrib>Radauer, Christian</creatorcontrib><creatorcontrib>O’Riordain, Gabriel</creatorcontrib><creatorcontrib>Laimer da Camara Machado, Margit</creatorcontrib><creatorcontrib>Scheiner, Otto</creatorcontrib><creatorcontrib>Breiteneder, Heimo</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>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>International archives of allergy and immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hoffmann-Sommergruber, Karin</au><au>Ferris, Rosemary</au><au>Pec, Martina</au><au>Radauer, Christian</au><au>O’Riordain, Gabriel</au><au>Laimer da Camara Machado, Margit</au><au>Scheiner, Otto</au><au>Breiteneder, Heimo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of Api g 1.0201, a New Member of the Api g 1 Family of Celery Allergens</atitle><jtitle>International archives of allergy and immunology</jtitle><addtitle>Int Arch Allergy Immunol</addtitle><date>2000-06-01</date><risdate>2000</risdate><volume>122</volume><issue>2</issue><spage>115</spage><epage>123</epage><pages>115-123</pages><issn>1018-2438</issn><eissn>1423-0097</eissn><abstract>Background: The association of pollinosis with allergy to plant foods occurs in up to 70% of tree pollen-allergic patients. In recent years, some of the relevant cross-reacting proteins have been characterized at the molecular and immunological level. Api g 1 has been identified as the celery homologue of the major birch pollen allergen, Bet v 1. Although a number of Bet v 1 isoforms have been characterized from birch pollen, little is known about isoforms of food allergens and their allergenic features. Methods: Api g 1.0201, an isoform of Api g 1, was isolated from a cDNA library, cloned and sequenced. The cDNA was expressed in Escherichia coli and the purified recombinant protein was tested in immunoblots. Results: Api g 1.0201 displays 72% sequence similarity to the previously identified Api g 1.0101 and consists of 159 amino acid residues. The sequence of Api g 1.0201 has five additional amino acid residues at the carboxy-terminus as compared to Api g 1.0101. Purified recombinant Api g 1.0201 is recognized by IgE from the sera of celery-allergic patients, as well as by the murine monoclonal anti-Bet v 1 antibody. In general, this isoform displays a weaker IgE-binding capacity than Api g 1.0101, as concluded from immunoblotting experiments. Results from inhibition assays revealed that IgE-binding to Api g 1.0201 is only slightly reduced by preincubation with either purified recombinant Api g 1.0101 or purified recombinant Bet v 1a. Total inhibition was only achieved when using purified natural Bet v 1. Conclusions: At present, little is known about the IgE-binding capacity of isoforms of Bet v 1 homologues of food allergens. Identification and characterization of such isoforms may help to contribute to a better understanding of food allergy and the observed cross-reactivity to pollen allergy.</abstract><cop>Basel, Switzerland</cop><pub>Karger</pub><pmid>10878490</pmid><doi>10.1159/000024367</doi><tpages>9</tpages></addata></record> |
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subjects | Allergens - chemistry Allergens - genetics Allergens - immunology Allergic diseases Amino Acid Sequence Antibodies, Monoclonal - immunology Antigens, Plant Api g 1 antigen Apiaceae - chemistry Apiaceae - genetics Apiaceae - immunology Apium graveolens dulce Base Sequence Biological and medical sciences Cloning, Molecular DNA, Complementary - analysis DNA, Complementary - genetics Escherichia coli - genetics Escherichia coli - metabolism Food Hypersensitivity - blood Food Hypersensitivity - immunology Humans Immunoblotting Immunoglobulin E - immunology Immunoglobulin E - metabolism Immunoglobulin G - immunology Immunopathology Medical sciences Models, Molecular Molecular Sequence Data Original Paper Other localizations Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - immunology Protein Isoforms Sequence Homology, Amino Acid |
title | Characterization of Api g 1.0201, a New Member of the Api g 1 Family of Celery Allergens |
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