Characterization of a new oriental-mustard (Brassica juncea) allergen, Bra j IE : detection of an allergenic epitope
Bra j IE, a major allergen from oriental-mustard (Brassica juncea) seeds, has been isolated and characterized. Its primary structure has been elucidated. This protein is composed of two chains (37 and 92 amino acids) linked by disulphide bridges. The amino acid sequence obtained is closely related t...
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| Veröffentlicht in: | Biochemical journal 1993-08, Vol.293 (3), p.625-632 |
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| container_title | Biochemical journal |
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| creator | MONSALVE, R. I GONZALEZ DE LA PENA, M. A MENENDEZ-ARIAS, L LOPEZ-OTIN, C VILLALBA, M RODRIGUEZ, R |
| description | Bra j IE, a major allergen from oriental-mustard (Brassica juncea) seeds, has been isolated and characterized. Its primary structure has been elucidated. This protein is composed of two chains (37 and 92 amino acids) linked by disulphide bridges. The amino acid sequence obtained is closely related to that previously determined for Sin a I, an allergen isolated from yellow mustard (Sinapis alba). A common epitope has been detected in the large chain of both Bra j IE and Sin a I by means of electroblotting and immunodetection with 2B3, which is a monoclonal antibody raised against the yellow-mustard allergen. A histidine residue of the large chain of both mustard allergens has been found to be essential for the recognition by 2B3 antibody. A synthetic multiantigenic peptide containing this His was recognized by 2B3 as well as by sera of mustard-hypersensitive individuals. Therefore this antigenic determinant must be involved in the allergenicity of these proteins. |
| doi_str_mv | 10.1042/bj2930625 |
| format | Article |
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I ; GONZALEZ DE LA PENA, M. A ; MENENDEZ-ARIAS, L ; LOPEZ-OTIN, C ; VILLALBA, M ; RODRIGUEZ, R</creator><creatorcontrib>MONSALVE, R. I ; GONZALEZ DE LA PENA, M. A ; MENENDEZ-ARIAS, L ; LOPEZ-OTIN, C ; VILLALBA, M ; RODRIGUEZ, R</creatorcontrib><description>Bra j IE, a major allergen from oriental-mustard (Brassica juncea) seeds, has been isolated and characterized. Its primary structure has been elucidated. This protein is composed of two chains (37 and 92 amino acids) linked by disulphide bridges. The amino acid sequence obtained is closely related to that previously determined for Sin a I, an allergen isolated from yellow mustard (Sinapis alba). A common epitope has been detected in the large chain of both Bra j IE and Sin a I by means of electroblotting and immunodetection with 2B3, which is a monoclonal antibody raised against the yellow-mustard allergen. A histidine residue of the large chain of both mustard allergens has been found to be essential for the recognition by 2B3 antibody. A synthetic multiantigenic peptide containing this His was recognized by 2B3 as well as by sera of mustard-hypersensitive individuals. Therefore this antigenic determinant must be involved in the allergenicity of these proteins.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2930625</identifier><identifier>PMID: 7688955</identifier><language>eng</language><publisher>Colchester: Portland Press</publisher><subject>2S Albumins, Plant ; Albumins - chemistry ; Albumins - immunology ; Albumins - isolation & purification ; Allergens - chemistry ; Allergens - immunology ; Allergens - isolation & purification ; Amino Acid Sequence ; Antibodies, Monoclonal - immunology ; Antigens, allergens ; Biological and medical sciences ; Blood ; Brassica - immunology ; Chromatography, High Pressure Liquid ; Epitopes - analysis ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; Immediate hypersensitivity. Allergy. Anaphylaxis, etc ; Immunobiology ; Molecular Sequence Data ; Plant Proteins - chemistry ; Plant Proteins - immunology ; Plant Proteins - isolation & purification</subject><ispartof>Biochemical journal, 1993-08, Vol.293 (3), p.625-632</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-c1f6050823aaa405d15e7afbad8baed75a3ed444a61a72d0be353c6b31ab0cf43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134412/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134412/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4854541$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7688955$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MONSALVE, R. I</creatorcontrib><creatorcontrib>GONZALEZ DE LA PENA, M. A</creatorcontrib><creatorcontrib>MENENDEZ-ARIAS, L</creatorcontrib><creatorcontrib>LOPEZ-OTIN, C</creatorcontrib><creatorcontrib>VILLALBA, M</creatorcontrib><creatorcontrib>RODRIGUEZ, R</creatorcontrib><title>Characterization of a new oriental-mustard (Brassica juncea) allergen, Bra j IE : detection of an allergenic epitope</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Bra j IE, a major allergen from oriental-mustard (Brassica juncea) seeds, has been isolated and characterized. Its primary structure has been elucidated. This protein is composed of two chains (37 and 92 amino acids) linked by disulphide bridges. The amino acid sequence obtained is closely related to that previously determined for Sin a I, an allergen isolated from yellow mustard (Sinapis alba). A common epitope has been detected in the large chain of both Bra j IE and Sin a I by means of electroblotting and immunodetection with 2B3, which is a monoclonal antibody raised against the yellow-mustard allergen. A histidine residue of the large chain of both mustard allergens has been found to be essential for the recognition by 2B3 antibody. A synthetic multiantigenic peptide containing this His was recognized by 2B3 as well as by sera of mustard-hypersensitive individuals. Therefore this antigenic determinant must be involved in the allergenicity of these proteins.</description><subject>2S Albumins, Plant</subject><subject>Albumins - chemistry</subject><subject>Albumins - immunology</subject><subject>Albumins - isolation & purification</subject><subject>Allergens - chemistry</subject><subject>Allergens - immunology</subject><subject>Allergens - isolation & purification</subject><subject>Amino Acid Sequence</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antigens, allergens</subject><subject>Biological and medical sciences</subject><subject>Blood</subject><subject>Brassica - immunology</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Epitopes - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Humans</subject><subject>Immediate hypersensitivity. Allergy. Anaphylaxis, etc</subject><subject>Immunobiology</subject><subject>Molecular Sequence Data</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - immunology</subject><subject>Plant Proteins - isolation & purification</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkV2LEzEUhoOs1Lp64Q8QcrEsLjiaz8l0LwQtVQsFb_Q6nMmc6aZMk5pkFP31jrQMepWL9-E5J-cl5AVnbzhT4m17ECvJaqEfkSVXhlWNEc0VWTJRq6pmgj8hT3M-MMYVU2xBFqZumpXWS1LWD5DAFUz-NxQfA409BRrwJ43JYygwVMcxF0gdffUhQc7eAT2MwSHcURgGTHsMr-kU0QPdbug97bCgm1VhhryjePIlnvAZedzDkPH55b0m3z5uvq4_V7svn7br97vKydWqVI73NdOsERIAFNMd12igb6FrWsDOaJDYKaWg5mBEx1qUWrq6lRxa5nolr8m7s_c0tkfs3PSdBIM9JX-E9MtG8Pb_JPgHu48_LOdSKS4mwe1FkOL3EXOxR58dDgMEjGO2Rk9XbIyZwLsz6FLMOWE_D-HM_q3IzhVN7Mt_t5rJSydTfnPJITsY-gTB-TxjqtFKKy7_APTFmrk</recordid><startdate>19930801</startdate><enddate>19930801</enddate><creator>MONSALVE, R. I</creator><creator>GONZALEZ DE LA PENA, M. A</creator><creator>MENENDEZ-ARIAS, L</creator><creator>LOPEZ-OTIN, C</creator><creator>VILLALBA, M</creator><creator>RODRIGUEZ, R</creator><general>Portland Press</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19930801</creationdate><title>Characterization of a new oriental-mustard (Brassica juncea) allergen, Bra j IE : detection of an allergenic epitope</title><author>MONSALVE, R. I ; GONZALEZ DE LA PENA, M. A ; MENENDEZ-ARIAS, L ; LOPEZ-OTIN, C ; VILLALBA, M ; RODRIGUEZ, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-c1f6050823aaa405d15e7afbad8baed75a3ed444a61a72d0be353c6b31ab0cf43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>2S Albumins, Plant</topic><topic>Albumins - chemistry</topic><topic>Albumins - immunology</topic><topic>Albumins - isolation & purification</topic><topic>Allergens - chemistry</topic><topic>Allergens - immunology</topic><topic>Allergens - isolation & purification</topic><topic>Amino Acid Sequence</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antigens, allergens</topic><topic>Biological and medical sciences</topic><topic>Blood</topic><topic>Brassica - immunology</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Epitopes - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Humans</topic><topic>Immediate hypersensitivity. Allergy. Anaphylaxis, etc</topic><topic>Immunobiology</topic><topic>Molecular Sequence Data</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - immunology</topic><topic>Plant Proteins - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MONSALVE, R. I</creatorcontrib><creatorcontrib>GONZALEZ DE LA PENA, M. A</creatorcontrib><creatorcontrib>MENENDEZ-ARIAS, L</creatorcontrib><creatorcontrib>LOPEZ-OTIN, C</creatorcontrib><creatorcontrib>VILLALBA, M</creatorcontrib><creatorcontrib>RODRIGUEZ, R</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MONSALVE, R. I</au><au>GONZALEZ DE LA PENA, M. A</au><au>MENENDEZ-ARIAS, L</au><au>LOPEZ-OTIN, C</au><au>VILLALBA, M</au><au>RODRIGUEZ, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a new oriental-mustard (Brassica juncea) allergen, Bra j IE : detection of an allergenic epitope</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1993-08-01</date><risdate>1993</risdate><volume>293</volume><issue>3</issue><spage>625</spage><epage>632</epage><pages>625-632</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Bra j IE, a major allergen from oriental-mustard (Brassica juncea) seeds, has been isolated and characterized. Its primary structure has been elucidated. This protein is composed of two chains (37 and 92 amino acids) linked by disulphide bridges. The amino acid sequence obtained is closely related to that previously determined for Sin a I, an allergen isolated from yellow mustard (Sinapis alba). A common epitope has been detected in the large chain of both Bra j IE and Sin a I by means of electroblotting and immunodetection with 2B3, which is a monoclonal antibody raised against the yellow-mustard allergen. A histidine residue of the large chain of both mustard allergens has been found to be essential for the recognition by 2B3 antibody. A synthetic multiantigenic peptide containing this His was recognized by 2B3 as well as by sera of mustard-hypersensitive individuals. Therefore this antigenic determinant must be involved in the allergenicity of these proteins.</abstract><cop>Colchester</cop><pub>Portland Press</pub><pmid>7688955</pmid><doi>10.1042/bj2930625</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 2S Albumins, Plant Albumins - chemistry Albumins - immunology Albumins - isolation & purification Allergens - chemistry Allergens - immunology Allergens - isolation & purification Amino Acid Sequence Antibodies, Monoclonal - immunology Antigens, allergens Biological and medical sciences Blood Brassica - immunology Chromatography, High Pressure Liquid Epitopes - analysis Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immediate hypersensitivity. Allergy. Anaphylaxis, etc Immunobiology Molecular Sequence Data Plant Proteins - chemistry Plant Proteins - immunology Plant Proteins - isolation & purification |
| title | Characterization of a new oriental-mustard (Brassica juncea) allergen, Bra j IE : detection of an allergenic epitope |
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