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
Hauptverfasser: 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
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container_end_page 1363
container_issue 10
container_start_page 1354
container_title Clinical and experimental allergy
container_volume 48
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
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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. 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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 &amp; 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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