Tropomyosins in mosquito and house dust mite cross‐react at the humoral and cellular level
Summary Background Aedes aegypti and Dermatophagoides pteronyssinus contain important allergens including cross‐reactive tropomyosins. However, the functional and clinical relevance of their cross‐reactivity is still debated. Objective To analyse the humoral and cellular cross‐reactivity of recombin...
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Veröffentlicht in: | Clinical and experimental allergy 2018-10, Vol.48 (10), p.1354-1363 |
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creator | Cantillo, Jose F. Puerta, Leonardo Fernandez‐Caldas, Enrique Subiza, Jose L. Soria, Irene Wöhrl, Stefan Ebner, Christof Keller, Walter Resch‐Marat, Yvonne Vrtala, Susanne Bohle, Barbara |
description | Summary
Background
Aedes aegypti and Dermatophagoides pteronyssinus contain important allergens including cross‐reactive tropomyosins. However, the functional and clinical relevance of their cross‐reactivity is still debated.
Objective
To analyse the humoral and cellular cross‐reactivity of recombinant Aed a 10.01, Aed a 10.02 and Der p 10.
Methods
Sera from 15 Austrian house dust mite‐allergic, Der p 10‐sensitized individuals were tested for IgE reactivity to recombinant tropomyosins in ELISA, inhibition ELISA and basophil activation tests. BALB/c mice were immunized with Aed a 10.01 or Aed a 10.02, and their sera were assessed for reactivity to all tropomyosins. Splenocytes were stimulated with all tropomyosins and synthetic peptides representing the amino acid sequence of Aed a 10.01.
Results
IgE antibodies of Der p 10‐sensitized patients cross‐reacted with both tropomyosins from A. aegypti. Aed a 10.01 was a more potent inhibitor of IgE binding to Der p 10 and a stronger activator of basophils sensitized with Der p 10‐specific IgE than Aed a 10.02. Murine antibodies raised against Aed a 10.01 and Aed a 10.02 cross‐reacted with Der p 10. Aed a 10.01‐specific antibody showed stronger cross‐reactivity with Der p 10 than Aed a 10.02‐specific antibody. Splenocytes from both groups of mice proliferated similarly to all tropomyosins. Five cross‐reactive T cell‐activating regions were identified.
Conclusion and Clinical relevance
Tropomyosins from D. pteronyssinus and A. aegypti show humoral and cellular cross‐reactivity, involving 5 potential T cell‐activating regions. The more pronounced cross‐reactivity of Aed a 10.01 and Der p 10 matched the higher sequence similarity of both proteins. |
doi_str_mv | 10.1111/cea.13229 |
format | Article |
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Background
Aedes aegypti and Dermatophagoides pteronyssinus contain important allergens including cross‐reactive tropomyosins. However, the functional and clinical relevance of their cross‐reactivity is still debated.
Objective
To analyse the humoral and cellular cross‐reactivity of recombinant Aed a 10.01, Aed a 10.02 and Der p 10.
Methods
Sera from 15 Austrian house dust mite‐allergic, Der p 10‐sensitized individuals were tested for IgE reactivity to recombinant tropomyosins in ELISA, inhibition ELISA and basophil activation tests. BALB/c mice were immunized with Aed a 10.01 or Aed a 10.02, and their sera were assessed for reactivity to all tropomyosins. Splenocytes were stimulated with all tropomyosins and synthetic peptides representing the amino acid sequence of Aed a 10.01.
Results
IgE antibodies of Der p 10‐sensitized patients cross‐reacted with both tropomyosins from A. aegypti. Aed a 10.01 was a more potent inhibitor of IgE binding to Der p 10 and a stronger activator of basophils sensitized with Der p 10‐specific IgE than Aed a 10.02. Murine antibodies raised against Aed a 10.01 and Aed a 10.02 cross‐reacted with Der p 10. Aed a 10.01‐specific antibody showed stronger cross‐reactivity with Der p 10 than Aed a 10.02‐specific antibody. Splenocytes from both groups of mice proliferated similarly to all tropomyosins. Five cross‐reactive T cell‐activating regions were identified.
Conclusion and Clinical relevance
Tropomyosins from D. pteronyssinus and A. aegypti show humoral and cellular cross‐reactivity, involving 5 potential T cell‐activating regions. The more pronounced cross‐reactivity of Aed a 10.01 and Der p 10 matched the higher sequence similarity of both proteins.</description><identifier>ISSN: 0954-7894</identifier><identifier>EISSN: 1365-2222</identifier><identifier>DOI: 10.1111/cea.13229</identifier><identifier>PMID: 29992665</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Aedes aegypti ; Allergens ; Amino acid sequence ; cross‐reactivity ; Dust ; Enzyme-linked immunosorbent assay ; House dust ; house dust mites ; Immunoglobulin E ; Leukocytes (basophilic) ; Lymphocytes ; Lymphocytes T ; Mice ; Mites ; mosquito ; Peptides ; Proteins ; Reactivity ; Splenocytes ; Synthetic peptides ; tropomyosin ; T‐cell epitopes</subject><ispartof>Clinical and experimental allergy, 2018-10, Vol.48 (10), p.1354-1363</ispartof><rights>2018 The Authors. Published by 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-c3889-ab85bb6db955e2f7a4798bdb501e76c6d94d93f0a4e06607ba889e33bfa7cb3d3</citedby><cites>FETCH-LOGICAL-c3889-ab85bb6db955e2f7a4798bdb501e76c6d94d93f0a4e06607ba889e33bfa7cb3d3</cites><orcidid>0000-0002-5105-7985</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.13229$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fcea.13229$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>314,777,781,1412,27905,27906,45555,45556</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29992665$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cantillo, Jose F.</creatorcontrib><creatorcontrib>Puerta, Leonardo</creatorcontrib><creatorcontrib>Fernandez‐Caldas, Enrique</creatorcontrib><creatorcontrib>Subiza, Jose L.</creatorcontrib><creatorcontrib>Soria, Irene</creatorcontrib><creatorcontrib>Wöhrl, Stefan</creatorcontrib><creatorcontrib>Ebner, Christof</creatorcontrib><creatorcontrib>Keller, Walter</creatorcontrib><creatorcontrib>Resch‐Marat, Yvonne</creatorcontrib><creatorcontrib>Vrtala, Susanne</creatorcontrib><creatorcontrib>Bohle, Barbara</creatorcontrib><title>Tropomyosins in mosquito and house dust mite cross‐react at the humoral and cellular level</title><title>Clinical and experimental allergy</title><addtitle>Clin Exp Allergy</addtitle><description>Summary
Background
Aedes aegypti and Dermatophagoides pteronyssinus contain important allergens including cross‐reactive tropomyosins. However, the functional and clinical relevance of their cross‐reactivity is still debated.
Objective
To analyse the humoral and cellular cross‐reactivity of recombinant Aed a 10.01, Aed a 10.02 and Der p 10.
Methods
Sera from 15 Austrian house dust mite‐allergic, Der p 10‐sensitized individuals were tested for IgE reactivity to recombinant tropomyosins in ELISA, inhibition ELISA and basophil activation tests. BALB/c mice were immunized with Aed a 10.01 or Aed a 10.02, and their sera were assessed for reactivity to all tropomyosins. Splenocytes were stimulated with all tropomyosins and synthetic peptides representing the amino acid sequence of Aed a 10.01.
Results
IgE antibodies of Der p 10‐sensitized patients cross‐reacted with both tropomyosins from A. aegypti. Aed a 10.01 was a more potent inhibitor of IgE binding to Der p 10 and a stronger activator of basophils sensitized with Der p 10‐specific IgE than Aed a 10.02. Murine antibodies raised against Aed a 10.01 and Aed a 10.02 cross‐reacted with Der p 10. Aed a 10.01‐specific antibody showed stronger cross‐reactivity with Der p 10 than Aed a 10.02‐specific antibody. Splenocytes from both groups of mice proliferated similarly to all tropomyosins. Five cross‐reactive T cell‐activating regions were identified.
Conclusion and Clinical relevance
Tropomyosins from D. pteronyssinus and A. aegypti show humoral and cellular cross‐reactivity, involving 5 potential T cell‐activating regions. The more pronounced cross‐reactivity of Aed a 10.01 and Der p 10 matched the higher sequence similarity of both proteins.</description><subject>Aedes aegypti</subject><subject>Allergens</subject><subject>Amino acid sequence</subject><subject>cross‐reactivity</subject><subject>Dust</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>House dust</subject><subject>house dust mites</subject><subject>Immunoglobulin E</subject><subject>Leukocytes (basophilic)</subject><subject>Lymphocytes</subject><subject>Lymphocytes T</subject><subject>Mice</subject><subject>Mites</subject><subject>mosquito</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Reactivity</subject><subject>Splenocytes</subject><subject>Synthetic peptides</subject><subject>tropomyosin</subject><subject>T‐cell epitopes</subject><issn>0954-7894</issn><issn>1365-2222</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><recordid>eNp1kL1OwzAURi0EoqUw8ALIEgsMoY6dOPFYVeVHqsRSNiTLTm7UVEnc2gmoG4_AM_IkuE1hQOIudznf0b0fQpchuQv9jDNQdyGjVByhYch4HFA_x2hIRBwFSSqiATpzbkUIYbFIT9GACiEo5_EQvS6sWZt6a1zZOFw2uDZu05WtwarJ8dJ0DnDeuRbXZQs4s8a5r49PCyprsWpxuwS87GpjVbUPZFBVXaUsruANqnN0UqjKwcVhj9DL_WwxfQzmzw9P08k8yFiaikDpNNaa51rEMdAiUVEiUp3rmISQ8IznIsoFK4iKgHBOEq18ChjThUoyzXI2Qje9d23NpgPXyrp0u1NUA_4DSQlPWeR1xKPXf9CV6Wzjr5M0DGnCCRHCU7c9tX_YQiHXtqyV3cqQyF3l0lcu95V79upg7HQN-S_507EHxj3wXlaw_d8kp7NJr_wGtdaL7g</recordid><startdate>201810</startdate><enddate>201810</enddate><creator>Cantillo, Jose F.</creator><creator>Puerta, Leonardo</creator><creator>Fernandez‐Caldas, Enrique</creator><creator>Subiza, Jose L.</creator><creator>Soria, Irene</creator><creator>Wöhrl, Stefan</creator><creator>Ebner, Christof</creator><creator>Keller, Walter</creator><creator>Resch‐Marat, Yvonne</creator><creator>Vrtala, Susanne</creator><creator>Bohle, Barbara</creator><general>Wiley Subscription Services, Inc</general><scope>24P</scope><scope>WIN</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>K9.</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-5105-7985</orcidid></search><sort><creationdate>201810</creationdate><title>Tropomyosins in mosquito and house dust mite cross‐react at the humoral and cellular level</title><author>Cantillo, Jose F. ; Puerta, Leonardo ; Fernandez‐Caldas, Enrique ; Subiza, Jose L. ; Soria, Irene ; Wöhrl, Stefan ; Ebner, Christof ; Keller, Walter ; Resch‐Marat, Yvonne ; Vrtala, Susanne ; Bohle, Barbara</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3889-ab85bb6db955e2f7a4798bdb501e76c6d94d93f0a4e06607ba889e33bfa7cb3d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Aedes aegypti</topic><topic>Allergens</topic><topic>Amino acid sequence</topic><topic>cross‐reactivity</topic><topic>Dust</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>House dust</topic><topic>house dust mites</topic><topic>Immunoglobulin E</topic><topic>Leukocytes (basophilic)</topic><topic>Lymphocytes</topic><topic>Lymphocytes T</topic><topic>Mice</topic><topic>Mites</topic><topic>mosquito</topic><topic>Peptides</topic><topic>Proteins</topic><topic>Reactivity</topic><topic>Splenocytes</topic><topic>Synthetic peptides</topic><topic>tropomyosin</topic><topic>T‐cell epitopes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cantillo, Jose F.</creatorcontrib><creatorcontrib>Puerta, Leonardo</creatorcontrib><creatorcontrib>Fernandez‐Caldas, Enrique</creatorcontrib><creatorcontrib>Subiza, Jose L.</creatorcontrib><creatorcontrib>Soria, Irene</creatorcontrib><creatorcontrib>Wöhrl, Stefan</creatorcontrib><creatorcontrib>Ebner, Christof</creatorcontrib><creatorcontrib>Keller, Walter</creatorcontrib><creatorcontrib>Resch‐Marat, Yvonne</creatorcontrib><creatorcontrib>Vrtala, Susanne</creatorcontrib><creatorcontrib>Bohle, Barbara</creatorcontrib><collection>Wiley Online Library Open Access</collection><collection>Wiley Free Content</collection><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><jtitle>Clinical and experimental allergy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cantillo, Jose F.</au><au>Puerta, Leonardo</au><au>Fernandez‐Caldas, Enrique</au><au>Subiza, Jose L.</au><au>Soria, Irene</au><au>Wöhrl, Stefan</au><au>Ebner, Christof</au><au>Keller, Walter</au><au>Resch‐Marat, Yvonne</au><au>Vrtala, Susanne</au><au>Bohle, Barbara</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tropomyosins in mosquito and house dust mite cross‐react at the humoral and cellular level</atitle><jtitle>Clinical and experimental allergy</jtitle><addtitle>Clin Exp Allergy</addtitle><date>2018-10</date><risdate>2018</risdate><volume>48</volume><issue>10</issue><spage>1354</spage><epage>1363</epage><pages>1354-1363</pages><issn>0954-7894</issn><eissn>1365-2222</eissn><abstract>Summary
Background
Aedes aegypti and Dermatophagoides pteronyssinus contain important allergens including cross‐reactive tropomyosins. However, the functional and clinical relevance of their cross‐reactivity is still debated.
Objective
To analyse the humoral and cellular cross‐reactivity of recombinant Aed a 10.01, Aed a 10.02 and Der p 10.
Methods
Sera from 15 Austrian house dust mite‐allergic, Der p 10‐sensitized individuals were tested for IgE reactivity to recombinant tropomyosins in ELISA, inhibition ELISA and basophil activation tests. BALB/c mice were immunized with Aed a 10.01 or Aed a 10.02, and their sera were assessed for reactivity to all tropomyosins. Splenocytes were stimulated with all tropomyosins and synthetic peptides representing the amino acid sequence of Aed a 10.01.
Results
IgE antibodies of Der p 10‐sensitized patients cross‐reacted with both tropomyosins from A. aegypti. Aed a 10.01 was a more potent inhibitor of IgE binding to Der p 10 and a stronger activator of basophils sensitized with Der p 10‐specific IgE than Aed a 10.02. Murine antibodies raised against Aed a 10.01 and Aed a 10.02 cross‐reacted with Der p 10. Aed a 10.01‐specific antibody showed stronger cross‐reactivity with Der p 10 than Aed a 10.02‐specific antibody. Splenocytes from both groups of mice proliferated similarly to all tropomyosins. Five cross‐reactive T cell‐activating regions were identified.
Conclusion and Clinical relevance
Tropomyosins from D. pteronyssinus and A. aegypti show humoral and cellular cross‐reactivity, involving 5 potential T cell‐activating regions. The more pronounced cross‐reactivity of Aed a 10.01 and Der p 10 matched the higher sequence similarity of both proteins.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>29992665</pmid><doi>10.1111/cea.13229</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-5105-7985</orcidid><oa>free_for_read</oa></addata></record> |
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source | Wiley Online Library Journals Frontfile Complete |
subjects | Aedes aegypti Allergens Amino acid sequence cross‐reactivity Dust Enzyme-linked immunosorbent assay House dust house dust mites Immunoglobulin E Leukocytes (basophilic) Lymphocytes Lymphocytes T Mice Mites mosquito Peptides Proteins Reactivity Splenocytes Synthetic peptides tropomyosin T‐cell epitopes |
title | Tropomyosins in mosquito and house dust mite cross‐react at the humoral and cellular level |
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