Isolation and biochemical characterization of a thaumatin-like kiwi allergen.
Identifieur interne : 000493 ( Main/Exploration ); précédent : 000492; suivant : 000494Isolation and biochemical characterization of a thaumatin-like kiwi allergen.
Auteurs : Marija Gavrovi Jankulovi [Yougoslavie] ; Tanja Irkovi ; Olga Vuckovi ; Marina Atanaskovi Markovi ; Arnd Petersen ; Gordana Gojgi ; Lidija Burazer ; Ratko M. JankovSource :
- The Journal of allergy and clinical immunology [ 0091-6749 ] ; 2002.
Descripteurs français
- KwdFr :
- Actinidia (immunologie), Allergènes (composition chimique), Allergènes (immunologie), Allergènes (isolement et purification), Antifongiques (composition chimique), Antifongiques (isolement et purification), Antifongiques (pharmacologie), Fruit (immunologie), Humains (MeSH), Hypersensibilité alimentaire (diagnostic), Hypersensibilité alimentaire (immunologie), Immunoglobuline E (immunologie), Masse moléculaire (MeSH), Point isoélectrique (MeSH), Protéines végétales (composition chimique), Protéines végétales (immunologie), Protéines végétales (isolement et purification), Séquence d'acides aminés (MeSH), Édulcorants (composition chimique).
- MESH :
- composition chimique : Allergènes, Antifongiques, Protéines végétales, Édulcorants.
- diagnostic : Hypersensibilité alimentaire.
- immunologie : Actinidia, Allergènes, Fruit, Hypersensibilité alimentaire, Immunoglobuline E, Protéines végétales.
- isolement et purification : Allergènes, Antifongiques, Protéines végétales.
- pharmacologie : Antifongiques.
- Humains, Masse moléculaire, Point isoélectrique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Actinidia (immunology), Allergens (chemistry), Allergens (immunology), Allergens (isolation & purification), Amino Acid Sequence (MeSH), Antifungal Agents (chemistry), Antifungal Agents (isolation & purification), Antifungal Agents (pharmacology), Food Hypersensitivity (diagnosis), Food Hypersensitivity (immunology), Fruit (immunology), Humans (MeSH), Immunoglobulin E (immunology), Isoelectric Point (MeSH), Molecular Weight (MeSH), Plant Proteins (chemistry), Plant Proteins (immunology), Plant Proteins (isolation & purification), Sweetening Agents (chemistry).
- MESH :
- chemical , chemistry : Allergens, Antifungal Agents, Plant Proteins, Sweetening Agents.
- diagnosis : Food Hypersensitivity.
- immunology : Actinidia, Allergens, Food Hypersensitivity, Fruit, Immunoglobulin E, Plant Proteins.
- chemical , isolation & purification : Allergens, Antifungal Agents, Plant Proteins.
- chemical , pharmacology : Antifungal Agents.
- Amino Acid Sequence, Humans, Isoelectric Point, Molecular Weight.
Abstract
BACKGROUND
Kiwi fruit allergy, as well as its association with hypersensitivity to other foods and to pollen, has been extensively reported in the last few years. Several IgE-binding components have been detected in kiwi extract, but only one 30- kd allergen has been isolated; it was identified as actinidin (Act c 1). Recently, we have reported a 24-kd kiwi protein to be a potential major allergen in a group of patients with oral allergy syndrome (OAS).
OBJECTIVE
The aim of this study was to purify and characterize the 24-kd kiwi allergen biochemically.
METHODS
Seven polysensitized patients with OAS to kiwi were used in this study. The kiwi allergen was isolated by using a combination of gel permeation, ion exchange, and immobilized metal ion affinity chromatography. Its biochemical characterization included determination of its isoelectric point, molecular weight, N-terminal sequencing, concanavalin A -binding ability, digestibility in simulated gastric fluid, and antifungal activity. Western blotting, 2-dimensional PAGE immunoblotting, and skin prick tests were performed to characterize the isolated protein immunochemically.
RESULTS
All 7 patients recognized the isolated 24-kd kiwi protein as an allergen. The isolated protein consisted of 2 isoforms with isoelectric points of 9.4 and 9.5 migrated as one protein band of 20 kd after SDS-PAGE under nonreducing conditions or at 24 kd under reducing conditions. The partial N-terminal sequence revealed that it is a thaumatin-like protein (TLP) with concanavalin A -binding ability. The protein showed antifungal activity toward Saccharomyces carlsbergensis, and Candida albicans. The protein was degraded by the simulated gastric fluid within 1 minute. Both isoforms bound IgE from a pool of sera in a 2-dimensional PAGE immunoblot. The TLP elicited positive skin prick test responses in 4 (80 %) of 5 patients with OAS.
CONCLUSION
This study reported isolation and full characterization of a new kiwi allergen, TLP (isoelectric points of 9.4 and 9.5 and molecular weight of 24 kd), which belongs to the family of pathogenesis-related proteins. The isolated protein expressed antifungal activity toward S carlsbergensis and C albicans.
DOI: 10.1067/mai.2002.128947
PubMed: 12417892
Affiliations:
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Jankov</name></author></analytic><series><title level="j">The Journal of allergy and clinical immunology</title><idno type="ISSN">0091-6749</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actinidia (immunology)</term><term>Allergens (chemistry)</term><term>Allergens (immunology)</term><term>Allergens (isolation & purification)</term><term>Amino Acid Sequence (MeSH)</term><term>Antifungal Agents (chemistry)</term><term>Antifungal Agents (isolation & purification)</term><term>Antifungal Agents (pharmacology)</term><term>Food Hypersensitivity (diagnosis)</term><term>Food Hypersensitivity (immunology)</term><term>Fruit (immunology)</term><term>Humans (MeSH)</term><term>Immunoglobulin E (immunology)</term><term>Isoelectric Point (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (immunology)</term><term>Plant Proteins (isolation & purification)</term><term>Sweetening Agents (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Actinidia (immunologie)</term><term>Allergènes (composition chimique)</term><term>Allergènes (immunologie)</term><term>Allergènes (isolement et purification)</term><term>Antifongiques (composition chimique)</term><term>Antifongiques (isolement et purification)</term><term>Antifongiques (pharmacologie)</term><term>Fruit (immunologie)</term><term>Humains (MeSH)</term><term>Hypersensibilité alimentaire (diagnostic)</term><term>Hypersensibilité alimentaire (immunologie)</term><term>Immunoglobuline E (immunologie)</term><term>Masse moléculaire (MeSH)</term><term>Point isoélectrique (MeSH)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (immunologie)</term><term>Protéines végétales (isolement et purification)</term><term>Séquence d'acides aminés (MeSH)</term><term>Édulcorants (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Allergens</term><term>Antifungal Agents</term><term>Plant Proteins</term><term>Sweetening Agents</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Allergènes</term><term>Antifongiques</term><term>Protéines végétales</term><term>Édulcorants</term></keywords><keywords scheme="MESH" qualifier="diagnosis" xml:lang="en"><term>Food Hypersensitivity</term></keywords><keywords scheme="MESH" qualifier="diagnostic" xml:lang="fr"><term>Hypersensibilité alimentaire</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Actinidia</term><term>Allergènes</term><term>Fruit</term><term>Hypersensibilité alimentaire</term><term>Immunoglobuline E</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Actinidia</term><term>Allergens</term><term>Food Hypersensitivity</term><term>Fruit</term><term>Immunoglobulin E</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Allergens</term><term>Antifungal Agents</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Allergènes</term><term>Antifongiques</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antifongiques</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antifungal Agents</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Humans</term><term>Isoelectric Point</term><term>Molecular Weight</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Masse moléculaire</term><term>Point isoélectrique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>Kiwi fruit allergy, as well as its association with hypersensitivity to other foods and to pollen, has been extensively reported in the last few years. Several IgE-binding components have been detected in kiwi extract, but only one 30- kd allergen has been isolated; it was identified as actinidin (Act c 1). Recently, we have reported a 24-kd kiwi protein to be a potential major allergen in a group of patients with oral allergy syndrome (OAS).</p></div><div type="abstract" xml:lang="en"><p><b>OBJECTIVE</b></p><p>The aim of this study was to purify and characterize the 24-kd kiwi allergen biochemically.</p></div><div type="abstract" xml:lang="en"><p><b>METHODS</b></p><p>Seven polysensitized patients with OAS to kiwi were used in this study. The kiwi allergen was isolated by using a combination of gel permeation, ion exchange, and immobilized metal ion affinity chromatography. Its biochemical characterization included determination of its isoelectric point, molecular weight, N-terminal sequencing, concanavalin A -binding ability, digestibility in simulated gastric fluid, and antifungal activity. Western blotting, 2-dimensional PAGE immunoblotting, and skin prick tests were performed to characterize the isolated protein immunochemically.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>All 7 patients recognized the isolated 24-kd kiwi protein as an allergen. The isolated protein consisted of 2 isoforms with isoelectric points of 9.4 and 9.5 migrated as one protein band of 20 kd after SDS-PAGE under nonreducing conditions or at 24 kd under reducing conditions. The partial N-terminal sequence revealed that it is a thaumatin-like protein (TLP) with concanavalin A -binding ability. The protein showed antifungal activity toward Saccharomyces carlsbergensis, and Candida albicans. The protein was degraded by the simulated gastric fluid within 1 minute. Both isoforms bound IgE from a pool of sera in a 2-dimensional PAGE immunoblot. The TLP elicited positive skin prick test responses in 4 (80 %) of 5 patients with OAS.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>This study reported isolation and full characterization of a new kiwi allergen, TLP (isoelectric points of 9.4 and 9.5 and molecular weight of 24 kd), which belongs to the family of pathogenesis-related proteins. The isolated protein expressed antifungal activity toward S carlsbergensis and C albicans.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12417892</PMID><DateCompleted><Year>2002</Year><Month>12</Month><Day>19</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>23</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0091-6749</ISSN><JournalIssue CitedMedium="Print"><Volume>110</Volume><Issue>5</Issue><PubDate><Year>2002</Year><Month>Nov</Month></PubDate></JournalIssue><Title>The Journal of allergy and clinical immunology</Title><ISOAbbreviation>J Allergy Clin Immunol</ISOAbbreviation></Journal><ArticleTitle>Isolation and biochemical characterization of a thaumatin-like kiwi allergen.</ArticleTitle><Pagination><MedlinePgn>805-10</MedlinePgn></Pagination><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Kiwi fruit allergy, as well as its association with hypersensitivity to other foods and to pollen, has been extensively reported in the last few years. Several IgE-binding components have been detected in kiwi extract, but only one 30- kd allergen has been isolated; it was identified as actinidin (Act c 1). Recently, we have reported a 24-kd kiwi protein to be a potential major allergen in a group of patients with oral allergy syndrome (OAS).</AbstractText><AbstractText Label="OBJECTIVE" NlmCategory="OBJECTIVE">The aim of this study was to purify and characterize the 24-kd kiwi allergen biochemically.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">Seven polysensitized patients with OAS to kiwi were used in this study. The kiwi allergen was isolated by using a combination of gel permeation, ion exchange, and immobilized metal ion affinity chromatography. Its biochemical characterization included determination of its isoelectric point, molecular weight, N-terminal sequencing, concanavalin A -binding ability, digestibility in simulated gastric fluid, and antifungal activity. Western blotting, 2-dimensional PAGE immunoblotting, and skin prick tests were performed to characterize the isolated protein immunochemically.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">All 7 patients recognized the isolated 24-kd kiwi protein as an allergen. The isolated protein consisted of 2 isoforms with isoelectric points of 9.4 and 9.5 migrated as one protein band of 20 kd after SDS-PAGE under nonreducing conditions or at 24 kd under reducing conditions. The partial N-terminal sequence revealed that it is a thaumatin-like protein (TLP) with concanavalin A -binding ability. The protein showed antifungal activity toward Saccharomyces carlsbergensis, and Candida albicans. The protein was degraded by the simulated gastric fluid within 1 minute. Both isoforms bound IgE from a pool of sera in a 2-dimensional PAGE immunoblot. The TLP elicited positive skin prick test responses in 4 (80 %) of 5 patients with OAS.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">This study reported isolation and full characterization of a new kiwi allergen, TLP (isoelectric points of 9.4 and 9.5 and molecular weight of 24 kd), which belongs to the family of pathogenesis-related proteins. The isolated protein expressed antifungal activity toward S carlsbergensis and C albicans.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gavrović-Jankulović</LastName><ForeName>Marija</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Chemistry, University of Belgrade, Yugoslavia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>ćIrković</LastName><ForeName>Tanja</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Vucković</LastName><ForeName>Olga</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Atanasković-Marković</LastName><ForeName>Marina</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Petersen</LastName><ForeName>Arnd</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Gojgić</LastName><ForeName>Gordana</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Burazer</LastName><ForeName>Lidija</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Jankov</LastName><ForeName>Ratko M</ForeName><Initials>RM</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Allergy Clin Immunol</MedlineTA><NlmUniqueID>1275002</NlmUniqueID><ISSNLinking>0091-6749</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000485">Allergens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013549">Sweetening Agents</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></ChemicalList><CitationSubset>AIM</CitationSubset><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D029042" MajorTopicYN="N">Actinidia</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000485" MajorTopicYN="N">Allergens</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><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="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005512" MajorTopicYN="N">Food Hypersensitivity</DescriptorName><QualifierName UI="Q000175" MajorTopicYN="N">diagnosis</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005638" MajorTopicYN="N">Fruit</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007073" MajorTopicYN="N">Immunoglobulin E</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007526" MajorTopicYN="N">Isoelectric Point</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013549" MajorTopicYN="N">Sweetening Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>11</Month><Day>6</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>12</Month><Day>20</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>11</Month><Day>6</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12417892</ArticleId><ArticleId IdType="pii">S009167490201432X</ArticleId><ArticleId IdType="doi">10.1067/mai.2002.128947</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Yougoslavie</li></country></list><tree><noCountry><name sortKey=" Irkovi, Tanja" sort=" Irkovi, Tanja" uniqKey=" Irkovi T" first="Tanja" last=" Irkovi">Tanja Irkovi</name><name sortKey="Atanaskovi Markovi, Marina" sort="Atanaskovi Markovi, Marina" uniqKey="Atanaskovi Markovi M" first="Marina" last="Atanaskovi Markovi">Marina Atanaskovi Markovi</name><name sortKey="Burazer, Lidija" sort="Burazer, Lidija" uniqKey="Burazer L" first="Lidija" last="Burazer">Lidija Burazer</name><name sortKey="Gojgi, Gordana" sort="Gojgi, Gordana" uniqKey="Gojgi G" first="Gordana" last="Gojgi">Gordana Gojgi</name><name sortKey="Jankov, Ratko M" sort="Jankov, Ratko M" uniqKey="Jankov R" first="Ratko M" last="Jankov">Ratko M. Jankov</name><name sortKey="Petersen, Arnd" sort="Petersen, Arnd" uniqKey="Petersen A" first="Arnd" last="Petersen">Arnd Petersen</name><name sortKey="Vuckovi, Olga" sort="Vuckovi, Olga" uniqKey="Vuckovi O" first="Olga" last="Vuckovi">Olga Vuckovi</name></noCountry><country name="Yougoslavie"><noRegion><name sortKey="Gavrovi Jankulovi, Marija" sort="Gavrovi Jankulovi, Marija" uniqKey="Gavrovi Jankulovi M" first="Marija" last="Gavrovi Jankulovi">Marija Gavrovi Jankulovi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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