Identification of thaumatin-like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa).
Identifieur interne : 000186 ( Main/Corpus ); précédent : 000185; suivant : 000187Identification of thaumatin-like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa).
Auteurs : Esther Mu Oz-García ; Olga Luengo-Sánchez ; Elisa Haroun-Díaz ; Aroa Sanz Maroto ; Arancha Palacín ; Araceli Díaz-Perales ; Manuel De Las Heras Gozalo ; Moisés Labrador-Horrillo ; Fernando Vivanco ; Javier Cuesta-Herranz ; Carlos Pastor-VargasSource :
- Molecular nutrition & food research [ 1613-4133 ] ; 2013.
English descriptors
- KwdEn :
- Adult (MeSH), Allergens (immunology), Allergens (isolation & purification), Amino Acid Sequence (MeSH), Aspartic Acid Proteases (immunology), Aspartic Acid Proteases (isolation & purification), Cross Reactions (immunology), Electrophoresis, Polyacrylamide Gel (MeSH), Female (MeSH), Food Hypersensitivity (immunology), Humans (MeSH), Immunoblotting (methods), Immunoglobulin E (metabolism), Lettuce (immunology), Male (MeSH), Middle Aged (MeSH), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), Plant Proteins (immunology), Plant Proteins (isolation & purification), Prunus (immunology), Young Adult (MeSH).
- MESH :
- chemical , immunology : Allergens, Aspartic Acid Proteases, Plant Proteins.
- chemical , isolation & purification : Allergens, Aspartic Acid Proteases, Plant Proteins.
- immunology : Cross Reactions, Food Hypersensitivity, Lettuce, Prunus.
- chemical , metabolism : Immunoglobulin E.
- methods : Immunoblotting.
- Adult, Amino Acid Sequence, Electrophoresis, Polyacrylamide Gel, Female, Humans, Male, Middle Aged, Molecular Sequence Data, Molecular Weight, Young Adult.
Abstract
SCOPE
Today, about 2-8% of the population of Western countries exhibits some type of food allergy whose impact ranges from localized symptoms confined to the oral mucosa to severe anaphylactic reactions. Consumed worldwide, lettuce is a Compositae family vegetable that can elicit allergic reactions. To date, however, only one lipid transfer protein has been described in allergic reaction to lettuce. The aim of this study was to identify potential new allergens involved in lettuce allergy.
METHODS AND RESULTS
Sera from 42 Spanish lettuce-allergic patients were obtained from patients recruited at the outpatient clinic. IgE-binding proteins were detected by SDS-PAGE and immunoblotting. Molecular characterization of IgE-binding bands was performed by MS. Thaumatin was purified using the Agilent 3100 OFFGEL system. The IgE-binding bands recognized in the sera of more than 50% of patients were identified as lipid transfer protein (9 kDa), a thaumatin-like protein (26 kDa), and an aspartyl protease (35 and 45 kDa). ELISA inhibition studies were performed to confirm the IgE reactivity of the purified allergen.
CONCLUSION
Two new major lettuce allergens-a thaumatin-like protein and an aspartyl protease-have been identified and characterized. These allergens may be used to improve both diagnosis and treatment of lettuce-allergic patients.
DOI: 10.1002/mnfr.201300139
PubMed: 23983075
Links to Exploration step
pubmed:23983075Le document en format XML
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sort="Palacin, Arancha" uniqKey="Palacin A" first="Arancha" last="Palacín">Arancha Palacín</name></author><author><name sortKey="Diaz Perales, Araceli" sort="Diaz Perales, Araceli" uniqKey="Diaz Perales A" first="Araceli" last="Díaz-Perales">Araceli Díaz-Perales</name></author><author><name sortKey="De Las Heras Gozalo, Manuel" sort="De Las Heras Gozalo, Manuel" uniqKey="De Las Heras Gozalo M" first="Manuel" last="De Las Heras Gozalo">Manuel De Las Heras Gozalo</name></author><author><name sortKey="Labrador Horrillo, Moises" sort="Labrador Horrillo, Moises" uniqKey="Labrador Horrillo M" first="Moisés" last="Labrador-Horrillo">Moisés Labrador-Horrillo</name></author><author><name sortKey="Vivanco, Fernando" sort="Vivanco, Fernando" uniqKey="Vivanco F" first="Fernando" last="Vivanco">Fernando Vivanco</name></author><author><name sortKey="Cuesta Herranz, Javier" sort="Cuesta Herranz, Javier" uniqKey="Cuesta Herranz J" first="Javier" last="Cuesta-Herranz">Javier Cuesta-Herranz</name></author><author><name sortKey="Pastor Vargas, Carlos" sort="Pastor Vargas, Carlos" uniqKey="Pastor Vargas C" first="Carlos" last="Pastor-Vargas">Carlos Pastor-Vargas</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23983075</idno><idno type="pmid">23983075</idno><idno type="doi">10.1002/mnfr.201300139</idno><idno type="wicri:Area/Main/Corpus">000186</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000186</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identification of thaumatin-like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa).</title><author><name sortKey="Mu Oz Garcia, Esther" sort="Mu Oz Garcia, Esther" uniqKey="Mu Oz Garcia E" first="Esther" last="Mu Oz-García">Esther Mu Oz-García</name><affiliation><nlm:affiliation>Department of Immunology, IIS- Fundación Jimenez Diaz, Madrid.</nlm:affiliation></affiliation></author><author><name sortKey="Luengo Sanchez, Olga" sort="Luengo Sanchez, Olga" uniqKey="Luengo Sanchez O" first="Olga" last="Luengo-Sánchez">Olga Luengo-Sánchez</name></author><author><name sortKey="Haroun Diaz, Elisa" sort="Haroun Diaz, Elisa" uniqKey="Haroun Diaz E" first="Elisa" last="Haroun-Díaz">Elisa Haroun-Díaz</name></author><author><name sortKey="Maroto, Aroa Sanz" sort="Maroto, Aroa Sanz" uniqKey="Maroto A" first="Aroa Sanz" last="Maroto">Aroa Sanz Maroto</name></author><author><name sortKey="Palacin, Arancha" sort="Palacin, Arancha" uniqKey="Palacin A" first="Arancha" last="Palacín">Arancha Palacín</name></author><author><name sortKey="Diaz Perales, Araceli" sort="Diaz Perales, Araceli" uniqKey="Diaz Perales A" first="Araceli" last="Díaz-Perales">Araceli Díaz-Perales</name></author><author><name sortKey="De Las Heras Gozalo, Manuel" sort="De Las Heras Gozalo, Manuel" uniqKey="De Las Heras Gozalo M" first="Manuel" last="De Las Heras Gozalo">Manuel De Las Heras Gozalo</name></author><author><name sortKey="Labrador Horrillo, Moises" sort="Labrador Horrillo, Moises" uniqKey="Labrador Horrillo M" first="Moisés" last="Labrador-Horrillo">Moisés Labrador-Horrillo</name></author><author><name sortKey="Vivanco, Fernando" sort="Vivanco, Fernando" uniqKey="Vivanco F" first="Fernando" last="Vivanco">Fernando Vivanco</name></author><author><name sortKey="Cuesta Herranz, Javier" sort="Cuesta Herranz, Javier" uniqKey="Cuesta Herranz J" first="Javier" last="Cuesta-Herranz">Javier Cuesta-Herranz</name></author><author><name sortKey="Pastor Vargas, Carlos" sort="Pastor Vargas, Carlos" uniqKey="Pastor Vargas C" first="Carlos" last="Pastor-Vargas">Carlos Pastor-Vargas</name></author></analytic><series><title level="j">Molecular nutrition & food research</title><idno type="eISSN">1613-4133</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adult (MeSH)</term><term>Allergens (immunology)</term><term>Allergens (isolation & purification)</term><term>Amino Acid Sequence (MeSH)</term><term>Aspartic Acid Proteases (immunology)</term><term>Aspartic Acid Proteases (isolation & purification)</term><term>Cross Reactions (immunology)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Female (MeSH)</term><term>Food Hypersensitivity (immunology)</term><term>Humans (MeSH)</term><term>Immunoblotting (methods)</term><term>Immunoglobulin E (metabolism)</term><term>Lettuce (immunology)</term><term>Male (MeSH)</term><term>Middle Aged (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Plant Proteins (immunology)</term><term>Plant Proteins (isolation & purification)</term><term>Prunus (immunology)</term><term>Young Adult (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Allergens</term><term>Aspartic Acid Proteases</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Allergens</term><term>Aspartic Acid Proteases</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Cross Reactions</term><term>Food Hypersensitivity</term><term>Lettuce</term><term>Prunus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Immunoglobulin E</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Immunoblotting</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adult</term><term>Amino Acid Sequence</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Female</term><term>Humans</term><term>Male</term><term>Middle Aged</term><term>Molecular Sequence Data</term><term>Molecular Weight</term><term>Young Adult</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>SCOPE</b></p><p>Today, about 2-8% of the population of Western countries exhibits some type of food allergy whose impact ranges from localized symptoms confined to the oral mucosa to severe anaphylactic reactions. Consumed worldwide, lettuce is a Compositae family vegetable that can elicit allergic reactions. To date, however, only one lipid transfer protein has been described in allergic reaction to lettuce. The aim of this study was to identify potential new allergens involved in lettuce allergy.</p></div><div type="abstract" xml:lang="en"><p><b>METHODS AND RESULTS</b></p><p>Sera from 42 Spanish lettuce-allergic patients were obtained from patients recruited at the outpatient clinic. IgE-binding proteins were detected by SDS-PAGE and immunoblotting. Molecular characterization of IgE-binding bands was performed by MS. Thaumatin was purified using the Agilent 3100 OFFGEL system. The IgE-binding bands recognized in the sera of more than 50% of patients were identified as lipid transfer protein (9 kDa), a thaumatin-like protein (26 kDa), and an aspartyl protease (35 and 45 kDa). ELISA inhibition studies were performed to confirm the IgE reactivity of the purified allergen.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>Two new major lettuce allergens-a thaumatin-like protein and an aspartyl protease-have been identified and characterized. These allergens may be used to improve both diagnosis and treatment of lettuce-allergic patients.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23983075</PMID><DateCompleted><Year>2014</Year><Month>09</Month><Day>02</Day></DateCompleted><DateRevised><Year>2013</Year><Month>12</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1613-4133</ISSN><JournalIssue CitedMedium="Internet"><Volume>57</Volume><Issue>12</Issue><PubDate><Year>2013</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Molecular nutrition & food research</Title><ISOAbbreviation>Mol Nutr Food Res</ISOAbbreviation></Journal><ArticleTitle>Identification of thaumatin-like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa).</ArticleTitle><Pagination><MedlinePgn>2245-52</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/mnfr.201300139</ELocationID><Abstract><AbstractText Label="SCOPE" NlmCategory="METHODS">Today, about 2-8% of the population of Western countries exhibits some type of food allergy whose impact ranges from localized symptoms confined to the oral mucosa to severe anaphylactic reactions. Consumed worldwide, lettuce is a Compositae family vegetable that can elicit allergic reactions. To date, however, only one lipid transfer protein has been described in allergic reaction to lettuce. The aim of this study was to identify potential new allergens involved in lettuce allergy.</AbstractText><AbstractText Label="METHODS AND RESULTS" NlmCategory="RESULTS">Sera from 42 Spanish lettuce-allergic patients were obtained from patients recruited at the outpatient clinic. IgE-binding proteins were detected by SDS-PAGE and immunoblotting. Molecular characterization of IgE-binding bands was performed by MS. Thaumatin was purified using the Agilent 3100 OFFGEL system. The IgE-binding bands recognized in the sera of more than 50% of patients were identified as lipid transfer protein (9 kDa), a thaumatin-like protein (26 kDa), and an aspartyl protease (35 and 45 kDa). ELISA inhibition studies were performed to confirm the IgE reactivity of the purified allergen.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">Two new major lettuce allergens-a thaumatin-like protein and an aspartyl protease-have been identified and characterized. These allergens may be used to improve both diagnosis and treatment of lettuce-allergic patients.</AbstractText><CopyrightInformation>© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Muñoz-García</LastName><ForeName>Esther</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Immunology, IIS- Fundación Jimenez Diaz, Madrid.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Luengo-Sánchez</LastName><ForeName>Olga</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Haroun-Díaz</LastName><ForeName>Elisa</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Maroto</LastName><ForeName>Aroa Sanz</ForeName><Initials>AS</Initials></Author><Author ValidYN="Y"><LastName>Palacín</LastName><ForeName>Arancha</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Díaz-Perales</LastName><ForeName>Araceli</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>de las Heras Gozalo</LastName><ForeName>Manuel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Labrador-Horrillo</LastName><ForeName>Moisés</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Vivanco</LastName><ForeName>Fernando</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Cuesta-Herranz</LastName><ForeName>Javier</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Pastor-Vargas</LastName><ForeName>Carlos</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>08</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Mol Nutr Food Res</MedlineTA><NlmUniqueID>101231818</NlmUniqueID><ISSNLinking>1613-4125</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000485">Allergens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>37341-29-0</RegistryNumber><NameOfSubstance UI="D007073">Immunoglobulin E</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D057055">Aspartic Acid Proteases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000328" MajorTopicYN="N">Adult</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000485" MajorTopicYN="N">Allergens</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057055" MajorTopicYN="N">Aspartic Acid Proteases</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003429" MajorTopicYN="N">Cross Reactions</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005512" MajorTopicYN="N">Food Hypersensitivity</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015151" MajorTopicYN="N">Immunoblotting</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007073" MajorTopicYN="N">Immunoglobulin E</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018545" MajorTopicYN="N">Lettuce</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008875" MajorTopicYN="N">Middle Aged</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D027861" MajorTopicYN="N">Prunus</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055815" MajorTopicYN="N">Young Adult</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Allergens</Keyword><Keyword MajorTopicYN="N">Aspartyl protease</Keyword><Keyword MajorTopicYN="N">Food allergy</Keyword><Keyword MajorTopicYN="N">Lettuce allergy</Keyword><Keyword MajorTopicYN="N">Thaumatin-like protein</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>02</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>05</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>06</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>8</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>8</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>9</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23983075</ArticleId><ArticleId 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