Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides
Summary Background Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactiv...
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| Veröffentlicht in: | Clinical and experimental allergy 2018-06, Vol.48 (6), p.731-740 |
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| creator | Prodic, I. Stanic‐Vucinic, D. Apostolovic, D. Mihailovic, J. Radibratovic, M. Radosavljevic, J. Burazer, L. Milcic, M. Smiljanic, K. Hage, M. Cirkovic Velickovic, T. |
| description | Summary
Background
Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion‐resistant peptides (SDRPs; |
| doi_str_mv | 10.1111/cea.13113 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_swepu</sourceid><recordid>TN_cdi_swepub_primary_oai_swepub_ki_se_490678</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2047382564</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4263-60c95812a7aae2c41e3a187ace677744b14f96bca06bf9e66b6941700a62af1d3</originalsourceid><addsrcrecordid>eNp1kcFu1DAQQCMEokvhwA8gS1zgkNZOvE7MrVotsFIlDsDZmngnW5fEXmynZW98Ah_DF_ElTMnSAxK-2PK8eZ7xFMVzwc8ErXOLcCZqIeoHxULUallWtB4WC66XsmxaLU-KJyldc87rpW4fFyeVlqKSbbsofm58P0zoLbLQsz2CnzIbIUf3jQXPUobODS4f7qIwDBh36BNznu0gEWR_ff-R3DgNkHHLtm6HlPGGVR8J7qbREQsRSUgZNnjK6KYcYmI5sHyFbLNbs4hgs7s5PpKuQsxHkwue_BGTI6vPVN4-uy2mp8WjHoaEz477afH57frT6n15-eHdZnVxWVpZqbpU3OplKypoALCyUmANom3AomqaRspOyF6rzgJXXa9RqU7RvzScg6qgF9v6tChnb7rF_dSZfXQjxIMJ4Mzx6gud0EjNVdMS_2rm9zF8nagBM7pkcRjAY5iSEVproaWSDaEv_0GvwxQ9dWMqTvG2WipJ1OuZsjGkFLG_L0Fwczd6Q6M3f0ZP7IujcepG3N6Tf2dNwPkM3LoBD_83mdX6Ylb-BktbvbM</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2047382564</pqid></control><display><type>article</type><title>Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides</title><source>Wiley Online Library Journals Frontfile Complete</source><source>SWEPUB Freely available online</source><creator>Prodic, I. ; Stanic‐Vucinic, D. ; Apostolovic, D. ; Mihailovic, J. ; Radibratovic, M. ; Radosavljevic, J. ; Burazer, L. ; Milcic, M. ; Smiljanic, K. ; Hage, M. ; Cirkovic Velickovic, T.</creator><creatorcontrib>Prodic, I. ; Stanic‐Vucinic, D. ; Apostolovic, D. ; Mihailovic, J. ; Radibratovic, M. ; Radosavljevic, J. ; Burazer, L. ; Milcic, M. ; Smiljanic, K. ; Hage, M. ; Cirkovic Velickovic, T.</creatorcontrib><description>Summary
Background
Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion‐resistant peptides (SDRPs; <10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated.
Objective
The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains.
Methods
Two‐dimensional gel‐based proteomics and shotgun peptidomics, immunoblotting with allergen‐specific antibodies from peanut‐sensitized patients, enzyme‐linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet‐circular dichroism spectroscopy were used to identify and characterize peanut digesta.
Results
Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion‐resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential.
Conclusion and Clinical Relevance
Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.</description><identifier>ISSN: 0954-7894</identifier><identifier>EISSN: 1365-2222</identifier><identifier>DOI: 10.1111/cea.13113</identifier><identifier>PMID: 29412488</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Allergens ; Ara h 1 antigen ; Ara h 2 antigen ; Ara h 3 antigen ; Circular dichroism ; Dichroism ; Digestion ; digestion‐resistant peptides ; Digestive system ; Epitopes ; Food allergies ; food matrix ; gastric‐simulated digestion ; Gastrointestinal tract ; Immune system ; Immunoblotting ; Immunoglobulin E ; peanut allergy ; Pepsin ; Peptides ; Proteins ; proteolysis resistance ; Proteomics ; Reactivity ; Sequences ; Spectroscopy</subject><ispartof>Clinical and experimental allergy, 2018-06, Vol.48 (6), p.731-740</ispartof><rights>2018 John Wiley & Sons Ltd</rights><rights>2018 John Wiley & Sons Ltd.</rights><rights>Copyright © 2018 John Wiley & Sons Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4263-60c95812a7aae2c41e3a187ace677744b14f96bca06bf9e66b6941700a62af1d3</citedby><cites>FETCH-LOGICAL-c4263-60c95812a7aae2c41e3a187ace677744b14f96bca06bf9e66b6941700a62af1d3</cites><orcidid>0000-0001-8388-6916 ; 0000-0003-2559-5234 ; 0000-0003-2576-3074 ; 0000-0003-0604-9246 ; 0000-0003-4774-8895</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fcea.13113$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fcea.13113$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,550,776,780,881,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29412488$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:138383631$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Prodic, I.</creatorcontrib><creatorcontrib>Stanic‐Vucinic, D.</creatorcontrib><creatorcontrib>Apostolovic, D.</creatorcontrib><creatorcontrib>Mihailovic, J.</creatorcontrib><creatorcontrib>Radibratovic, M.</creatorcontrib><creatorcontrib>Radosavljevic, J.</creatorcontrib><creatorcontrib>Burazer, L.</creatorcontrib><creatorcontrib>Milcic, M.</creatorcontrib><creatorcontrib>Smiljanic, K.</creatorcontrib><creatorcontrib>Hage, M.</creatorcontrib><creatorcontrib>Cirkovic Velickovic, T.</creatorcontrib><title>Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides</title><title>Clinical and experimental allergy</title><addtitle>Clin Exp Allergy</addtitle><description>Summary
Background
Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion‐resistant peptides (SDRPs; <10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated.
Objective
The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains.
Methods
Two‐dimensional gel‐based proteomics and shotgun peptidomics, immunoblotting with allergen‐specific antibodies from peanut‐sensitized patients, enzyme‐linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet‐circular dichroism spectroscopy were used to identify and characterize peanut digesta.
Results
Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion‐resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential.
Conclusion and Clinical Relevance
Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.</description><subject>Allergens</subject><subject>Ara h 1 antigen</subject><subject>Ara h 2 antigen</subject><subject>Ara h 3 antigen</subject><subject>Circular dichroism</subject><subject>Dichroism</subject><subject>Digestion</subject><subject>digestion‐resistant peptides</subject><subject>Digestive system</subject><subject>Epitopes</subject><subject>Food allergies</subject><subject>food matrix</subject><subject>gastric‐simulated digestion</subject><subject>Gastrointestinal tract</subject><subject>Immune system</subject><subject>Immunoblotting</subject><subject>Immunoglobulin E</subject><subject>peanut allergy</subject><subject>Pepsin</subject><subject>Peptides</subject><subject>Proteins</subject><subject>proteolysis resistance</subject><subject>Proteomics</subject><subject>Reactivity</subject><subject>Sequences</subject><subject>Spectroscopy</subject><issn>0954-7894</issn><issn>1365-2222</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>D8T</sourceid><recordid>eNp1kcFu1DAQQCMEokvhwA8gS1zgkNZOvE7MrVotsFIlDsDZmngnW5fEXmynZW98Ah_DF_ElTMnSAxK-2PK8eZ7xFMVzwc8ErXOLcCZqIeoHxULUallWtB4WC66XsmxaLU-KJyldc87rpW4fFyeVlqKSbbsofm58P0zoLbLQsz2CnzIbIUf3jQXPUobODS4f7qIwDBh36BNznu0gEWR_ff-R3DgNkHHLtm6HlPGGVR8J7qbREQsRSUgZNnjK6KYcYmI5sHyFbLNbs4hgs7s5PpKuQsxHkwue_BGTI6vPVN4-uy2mp8WjHoaEz477afH57frT6n15-eHdZnVxWVpZqbpU3OplKypoALCyUmANom3AomqaRspOyF6rzgJXXa9RqU7RvzScg6qgF9v6tChnb7rF_dSZfXQjxIMJ4Mzx6gud0EjNVdMS_2rm9zF8nagBM7pkcRjAY5iSEVproaWSDaEv_0GvwxQ9dWMqTvG2WipJ1OuZsjGkFLG_L0Fwczd6Q6M3f0ZP7IujcepG3N6Tf2dNwPkM3LoBD_83mdX6Ylb-BktbvbM</recordid><startdate>201806</startdate><enddate>201806</enddate><creator>Prodic, I.</creator><creator>Stanic‐Vucinic, D.</creator><creator>Apostolovic, D.</creator><creator>Mihailovic, J.</creator><creator>Radibratovic, M.</creator><creator>Radosavljevic, J.</creator><creator>Burazer, L.</creator><creator>Milcic, M.</creator><creator>Smiljanic, K.</creator><creator>Hage, M.</creator><creator>Cirkovic Velickovic, T.</creator><general>Wiley Subscription Services, Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>K9.</scope><scope>7X8</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8T</scope><scope>ZZAVC</scope><orcidid>https://orcid.org/0000-0001-8388-6916</orcidid><orcidid>https://orcid.org/0000-0003-2559-5234</orcidid><orcidid>https://orcid.org/0000-0003-2576-3074</orcidid><orcidid>https://orcid.org/0000-0003-0604-9246</orcidid><orcidid>https://orcid.org/0000-0003-4774-8895</orcidid></search><sort><creationdate>201806</creationdate><title>Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides</title><author>Prodic, I. ; Stanic‐Vucinic, D. ; Apostolovic, D. ; Mihailovic, J. ; Radibratovic, M. ; Radosavljevic, J. ; Burazer, L. ; Milcic, M. ; Smiljanic, K. ; Hage, M. ; Cirkovic Velickovic, T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4263-60c95812a7aae2c41e3a187ace677744b14f96bca06bf9e66b6941700a62af1d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Allergens</topic><topic>Ara h 1 antigen</topic><topic>Ara h 2 antigen</topic><topic>Ara h 3 antigen</topic><topic>Circular dichroism</topic><topic>Dichroism</topic><topic>Digestion</topic><topic>digestion‐resistant peptides</topic><topic>Digestive system</topic><topic>Epitopes</topic><topic>Food allergies</topic><topic>food matrix</topic><topic>gastric‐simulated digestion</topic><topic>Gastrointestinal tract</topic><topic>Immune system</topic><topic>Immunoblotting</topic><topic>Immunoglobulin E</topic><topic>peanut allergy</topic><topic>Pepsin</topic><topic>Peptides</topic><topic>Proteins</topic><topic>proteolysis resistance</topic><topic>Proteomics</topic><topic>Reactivity</topic><topic>Sequences</topic><topic>Spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Prodic, I.</creatorcontrib><creatorcontrib>Stanic‐Vucinic, D.</creatorcontrib><creatorcontrib>Apostolovic, D.</creatorcontrib><creatorcontrib>Mihailovic, J.</creatorcontrib><creatorcontrib>Radibratovic, M.</creatorcontrib><creatorcontrib>Radosavljevic, J.</creatorcontrib><creatorcontrib>Burazer, L.</creatorcontrib><creatorcontrib>Milcic, M.</creatorcontrib><creatorcontrib>Smiljanic, K.</creatorcontrib><creatorcontrib>Hage, M.</creatorcontrib><creatorcontrib>Cirkovic Velickovic, T.</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Freely available online</collection><collection>SwePub Articles full text</collection><jtitle>Clinical and experimental allergy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Prodic, I.</au><au>Stanic‐Vucinic, D.</au><au>Apostolovic, D.</au><au>Mihailovic, J.</au><au>Radibratovic, M.</au><au>Radosavljevic, J.</au><au>Burazer, L.</au><au>Milcic, M.</au><au>Smiljanic, K.</au><au>Hage, M.</au><au>Cirkovic Velickovic, T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides</atitle><jtitle>Clinical and experimental allergy</jtitle><addtitle>Clin Exp Allergy</addtitle><date>2018-06</date><risdate>2018</risdate><volume>48</volume><issue>6</issue><spage>731</spage><epage>740</epage><pages>731-740</pages><issn>0954-7894</issn><eissn>1365-2222</eissn><abstract>Summary
Background
Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion‐resistant peptides (SDRPs; <10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated.
Objective
The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains.
Methods
Two‐dimensional gel‐based proteomics and shotgun peptidomics, immunoblotting with allergen‐specific antibodies from peanut‐sensitized patients, enzyme‐linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet‐circular dichroism spectroscopy were used to identify and characterize peanut digesta.
Results
Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion‐resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential.
Conclusion and Clinical Relevance
Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>29412488</pmid><doi>10.1111/cea.13113</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-8388-6916</orcidid><orcidid>https://orcid.org/0000-0003-2559-5234</orcidid><orcidid>https://orcid.org/0000-0003-2576-3074</orcidid><orcidid>https://orcid.org/0000-0003-0604-9246</orcidid><orcidid>https://orcid.org/0000-0003-4774-8895</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Clinical and experimental allergy, 2018-06, Vol.48 (6), p.731-740 |
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| subjects | Allergens Ara h 1 antigen Ara h 2 antigen Ara h 3 antigen Circular dichroism Dichroism Digestion digestion‐resistant peptides Digestive system Epitopes Food allergies food matrix gastric‐simulated digestion Gastrointestinal tract Immune system Immunoblotting Immunoglobulin E peanut allergy Pepsin Peptides Proteins proteolysis resistance Proteomics Reactivity Sequences Spectroscopy |
| title | Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides |
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