The mapping of linear B‐cell epitope regions in the extracellular parts of the desmoglein 1 and 3 proteins: recognition of immobilized peptides by pemphigus patients' serum autoantibodies
Identifieur interne : 001B26 ( Istex/Corpus ); précédent : 001B25; suivant : 001B27The mapping of linear B‐cell epitope regions in the extracellular parts of the desmoglein 1 and 3 proteins: recognition of immobilized peptides by pemphigus patients' serum autoantibodies
Auteurs : Hajnalka Szabados ; Szilvia B Sze ; Pálma Sill ; Sarolta Kárpáti ; Ferenc Hudecz ; Katalin UraySource :
- Journal of Peptide Science [ 1075-2617 ] ; 2013-02.
Abstract
Desmosomal transmembrane glycoproteins desmogleins (Dsg) 1 and 3 are targets of life‐threatening autoimmune blistering disorders such as Pemphigus vulgaris (PV) and Pemphigus foliaceus (PF). In these diseases, pemphigus autoantibodies are produced against Dsg1 and Dsg3 proteins. The autoantibodies bind to these transmembrane elements leading to a loss of desmosomal cell–cell adhesion and clinically, to the presence of blisters and erosions. Identification, characterization, and detailed analysis of the binding sites of autoantibodies have an outstanding importance in understanding the immunopathology of the disease and also in the design of novel diagnostics. Here, we describe the localization of the B‐cell epitope regions of Dsg1 and Dsg3 proteins' extracellular parts recognized by IgG‐type serum autoantibodies of patients with PV and PF. In our study, overlapping pentadecapeptides were synthesized on hydroxypropyl methacrylate pins based on the results of in silico predictions. To detect the interaction between the serum autoantibodies and the immobilized synthetic peptides, modified Enzyme Linked Immunosorbent Assay (ELISA) was performed with pin‐attached peptides testing the serum samples of ten patients and four healthy donors. We identified five possible epitope regions (aa86‐110, aa196‐220, aa226‐250, aa326‐340, and aa486‐520) within the extracellular part of the Dsg1 and four possible epitope regions (aa64‐78, aa330‐344, aa375‐399, and aa446‐460) within that of the Dsg3 protein sequence using these methods. Our data showed that serum autoantibodies of patients, previously identified as Dsg1 and Dsg3 positive, are able to recognize continuous linear epitope regions of both Dsg1 and Dsg3 proteins using pin‐bound overlapping peptides in modified ELISAs. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.
Pemphigus specific epitope regions were identified in desmoglein 1 and 3 proteins with pin‐bound synthetic 15‐mer peptides and modified ELISAs by testing serum antibodies from patients and healthy donors. The serum antibodies of the healthy individuals did not show any specific recognition. Not only conformational but also linear epitope regions are spread in the entire extracellular region of the desmoglein 1 protein.
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DOI: 10.1002/psc.2476
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In these diseases, pemphigus autoantibodies are produced against Dsg1 and Dsg3 proteins. The autoantibodies bind to these transmembrane elements leading to a loss of desmosomal cell–cell adhesion and clinically, to the presence of blisters and erosions. Identification, characterization, and detailed analysis of the binding sites of autoantibodies have an outstanding importance in understanding the immunopathology of the disease and also in the design of novel diagnostics. Here, we describe the localization of the B‐cell epitope regions of Dsg1 and Dsg3 proteins' extracellular parts recognized by IgG‐type serum autoantibodies of patients with PV and PF. In our study, overlapping pentadecapeptides were synthesized on hydroxypropyl methacrylate pins based on the results of in silico predictions. To detect the interaction between the serum autoantibodies and the immobilized synthetic peptides, modified Enzyme Linked Immunosorbent Assay (ELISA) was performed with pin‐attached peptides testing the serum samples of ten patients and four healthy donors. We identified five possible epitope regions (aa86‐110, aa196‐220, aa226‐250, aa326‐340, and aa486‐520) within the extracellular part of the Dsg1 and four possible epitope regions (aa64‐78, aa330‐344, aa375‐399, and aa446‐460) within that of the Dsg3 protein sequence using these methods. Our data showed that serum autoantibodies of patients, previously identified as Dsg1 and Dsg3 positive, are able to recognize continuous linear epitope regions of both Dsg1 and Dsg3 proteins using pin‐bound overlapping peptides in modified ELISAs. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.</div><div type="abstract">Pemphigus specific epitope regions were identified in desmoglein 1 and 3 proteins with pin‐bound synthetic 15‐mer peptides and modified ELISAs by testing serum antibodies from patients and healthy donors. The serum antibodies of the healthy individuals did not show any specific recognition. 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In these diseases, pemphigus autoantibodies are produced against Dsg1 and Dsg3 proteins. The autoantibodies bind to these transmembrane elements leading to a loss of desmosomal cell–cell adhesion and clinically, to the presence of blisters and erosions. Identification, characterization, and detailed analysis of the binding sites of autoantibodies have an outstanding importance in understanding the immunopathology of the disease and also in the design of novel diagnostics. Here, we describe the localization of the B‐cell epitope regions of Dsg1 and Dsg3 proteins' extracellular parts recognized by IgG‐type serum autoantibodies of patients with PV and PF. In our study, overlapping pentadecapeptides were synthesized on hydroxypropyl methacrylate pins based on the results of in silico predictions. To detect the interaction between the serum autoantibodies and the immobilized synthetic peptides, modified Enzyme Linked Immunosorbent Assay (ELISA) was performed with pin‐attached peptides testing the serum samples of ten patients and four healthy donors. We identified five possible epitope regions (aa86‐110, aa196‐220, aa226‐250, aa326‐340, and aa486‐520) within the extracellular part of the Dsg1 and four possible epitope regions (aa64‐78, aa330‐344, aa375‐399, and aa446‐460) within that of the Dsg3 protein sequence using these methods. Our data showed that serum autoantibodies of patients, previously identified as Dsg1 and Dsg3 positive, are able to recognize continuous linear epitope regions of both Dsg1 and Dsg3 proteins using pin‐bound overlapping peptides in modified ELISAs. 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University</orgName><address><street>Budapest 112</street><postCode>PO Box 32 H‐1518</postCode><country key="HU" xml:lang="en">HUNGARY</country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">Szilvia</forename><surname>Bősze</surname></persName><affiliation><orgName type="division">Research Group of Peptide Chemistry, Hungarian Academy of Sciences</orgName><orgName type="institution">Eötvös L. University</orgName><address><street>Budapest 112</street><postCode>PO Box 32 H‐1518</postCode><country key="HU" xml:lang="en">HUNGARY</country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">Pálma</forename><surname>Silló</surname></persName><affiliation><orgName type="division">Department of Dermatology, Venereology and Dermato‐Oncology</orgName><orgName type="institution">Semmelweis University</orgName><address><settlement>Budapest</settlement><country key="HU" xml:lang="en">HUNGARY</country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">Sarolta</forename><surname>Kárpáti</surname></persName><affiliation><orgName type="division">Department of Dermatology, Venereology and Dermato‐Oncology</orgName><orgName type="institution">Semmelweis University</orgName><address><settlement>Budapest</settlement><country key="HU" xml:lang="en">HUNGARY</country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">Ferenc</forename><surname>Hudecz</surname></persName><affiliation><orgName type="division">Research Group of Peptide Chemistry, Hungarian Academy of Sciences</orgName><orgName type="institution">Eötvös L. University</orgName><address><street>Budapest 112</street><postCode>PO Box 32 H‐1518</postCode><country key="HU" xml:lang="en">HUNGARY</country></address></affiliation><affiliation><orgName type="division">Institute of Chemistry</orgName><orgName type="institution">Eötvös L. University</orgName><address><settlement>Budapest</settlement><country key="HU" xml:lang="en">HUNGARY</country></address></affiliation></author><author xml:id="author-0005" role="corresp"><persName><forename type="first">Katalin</forename><surname>Uray</surname></persName><affiliation><orgName type="division">Research Group of Peptide Chemistry, Hungarian Academy of Sciences</orgName><orgName type="institution">Eötvös L. 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<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract style="main"><p>Desmosomal transmembrane glycoproteins desmogleins (Dsg) 1 and 3 are targets of life‐threatening autoimmune blistering disorders such as <hi rend="italic">Pemphigus vulgaris</hi> (PV) and <hi rend="italic">Pemphigus foliaceus</hi> (PF). In these diseases, pemphigus autoantibodies are produced against Dsg1 and Dsg3 proteins. The autoantibodies bind to these transmembrane elements leading to a loss of desmosomal cell–cell adhesion and clinically, to the presence of blisters and erosions. Identification, characterization, and detailed analysis of the binding sites of autoantibodies have an outstanding importance in understanding the immunopathology of the disease and also in the design of novel diagnostics.</p><p>Here, we describe the localization of the B‐cell epitope regions of Dsg1 and Dsg3 proteins' extracellular parts recognized by IgG‐type serum autoantibodies of patients with PV and PF. In our study, overlapping pentadecapeptides were synthesized on hydroxypropyl methacrylate pins based on the results of <hi rend="italic">in silico</hi> predictions. To detect the interaction between the serum autoantibodies and the immobilized synthetic peptides, modified Enzyme Linked Immunosorbent Assay (ELISA) was performed with pin‐attached peptides testing the serum samples of ten patients and four healthy donors. We identified five possible epitope regions (aa86‐110, aa196‐220, aa226‐250, aa326‐340, and aa486‐520) within the extracellular part of the Dsg1 and four possible epitope regions (aa64‐78, aa330‐344, aa375‐399, and aa446‐460) within that of the Dsg3 protein sequence using these methods. Our data showed that serum autoantibodies of patients, previously identified as Dsg1 and Dsg3 positive, are able to recognize continuous linear epitope regions of both Dsg1 and Dsg3 proteins using pin‐bound overlapping peptides in modified ELISAs. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.</p></abstract><abstract style="graphical"><p>Pemphigus specific epitope regions were identified in desmoglein 1 and 3 proteins with pin‐bound synthetic 15‐mer peptides and modified ELISAs by testing serum antibodies from patients and healthy donors. The serum antibodies of the healthy individuals did not show any specific recognition. Not only conformational but also linear epitope regions are spread in the entire extracellular region of the desmoglein 1 protein.
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University, Budapest 112, PO Box 32, H‐1518, Hungary. E‐mail: <email>uray@elte.hu</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:PSC.PSC2476.pdf"></link></linkGroup></publicationMeta><contentMeta><titleGroup><title type="main">The mapping of linear B‐cell epitope regions in the extracellular parts of the desmoglein 1 and 3 proteins: recognition of immobilized peptides by pemphigus patients' serum autoantibodies</title><title type="short">LINEAR B‐CELL EPITOPE REGIONS IN DESMOGLEIN 1 AND 3 PROTEINS</title><title type="shortAuthors">SZABADOS <i>ET AL.</i></title></titleGroup><creators><creator creatorRole="author" xml:id="psc2476-cr-0001" affiliationRef="#psc2476-aff-0001"><personName><givenNames>Hajnalka</givenNames><familyName>Szabados</familyName></personName></creator><creator creatorRole="author" xml:id="psc2476-cr-0002" affiliationRef="#psc2476-aff-0001"><personName><givenNames>Szilvia</givenNames><familyName>Bősze</familyName></personName></creator><creator creatorRole="author" xml:id="psc2476-cr-0003" affiliationRef="#psc2476-aff-0002"><personName><givenNames>Pálma</givenNames><familyName>Silló</familyName></personName></creator><creator creatorRole="author" xml:id="psc2476-cr-0004" affiliationRef="#psc2476-aff-0002"><personName><givenNames>Sarolta</givenNames><familyName>Kárpáti</familyName></personName></creator><creator creatorRole="author" xml:id="psc2476-cr-0005" affiliationRef="#psc2476-aff-0001 #psc2476-aff-0003"><personName><givenNames>Ferenc</givenNames><familyName>Hudecz</familyName></personName></creator><creator creatorRole="author" xml:id="psc2476-cr-0006" affiliationRef="#psc2476-aff-0001" corresponding="yes"><personName><givenNames>Katalin</givenNames><familyName>Uray</familyName></personName></creator></creators><affiliationGroup><affiliation countryCode="HU" type="organization" xml:id="psc2476-aff-0001"><orgDiv>Research Group of Peptide Chemistry, Hungarian Academy of Sciences</orgDiv><orgName>Eötvös L. University</orgName><address><street>Budapest 112</street><postCode>PO Box 32 H‐1518</postCode><country>Hungary</country></address></affiliation><affiliation countryCode="HU" type="organization" xml:id="psc2476-aff-0002"><orgDiv>Department of Dermatology, Venereology and Dermato‐Oncology</orgDiv><orgName>Semmelweis University</orgName><address><city>Budapest</city><country>Hungary</country></address></affiliation><affiliation countryCode="HU" type="organization" xml:id="psc2476-aff-0003"><orgDiv>Institute of Chemistry</orgDiv><orgName>Eötvös L. University</orgName><address><city>Budapest</city><country>Hungary</country></address></affiliation></affiliationGroup><keywordGroup type="author"><keyword xml:id="psc2476-kwd-0001">autoantibody epitopes</keyword><keyword xml:id="psc2476-kwd-0002">pin‐bound peptides</keyword><keyword xml:id="psc2476-kwd-0003">modified ELISA</keyword><keyword xml:id="psc2476-kwd-0004">desmoglein 1 and 3</keyword><keyword xml:id="psc2476-kwd-0005">pemphigus</keyword></keywordGroup><abstractGroup><abstract type="main"><p>Desmosomal transmembrane glycoproteins desmogleins (Dsg) 1 and 3 are targets of life‐threatening autoimmune blistering disorders such as <i>Pemphigus vulgaris</i> (PV) and <i>Pemphigus foliaceus</i> (PF). In these diseases, pemphigus autoantibodies are produced against Dsg1 and Dsg3 proteins. The autoantibodies bind to these transmembrane elements leading to a loss of desmosomal cell–cell adhesion and clinically, to the presence of blisters and erosions. Identification, characterization, and detailed analysis of the binding sites of autoantibodies have an outstanding importance in understanding the immunopathology of the disease and also in the design of novel diagnostics.</p><p>Here, we describe the localization of the B‐cell epitope regions of Dsg1 and Dsg3 proteins' extracellular parts recognized by IgG‐type serum autoantibodies of patients with PV and PF. In our study, overlapping pentadecapeptides were synthesized on hydroxypropyl methacrylate pins based on the results of <i>in silico</i> predictions. To detect the interaction between the serum autoantibodies and the immobilized synthetic peptides, modified Enzyme Linked Immunosorbent Assay (ELISA) was performed with pin‐attached peptides testing the serum samples of ten patients and four healthy donors. We identified five possible epitope regions (aa86‐110, aa196‐220, aa226‐250, aa326‐340, and aa486‐520) within the extracellular part of the Dsg1 and four possible epitope regions (aa64‐78, aa330‐344, aa375‐399, and aa446‐460) within that of the Dsg3 protein sequence using these methods. Our data showed that serum autoantibodies of patients, previously identified as Dsg1 and Dsg3 positive, are able to recognize continuous linear epitope regions of both Dsg1 and Dsg3 proteins using pin‐bound overlapping peptides in modified ELISAs. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.</p></abstract><abstract type="graphical"><p>Pemphigus specific epitope regions were identified in desmoglein 1 and 3 proteins with pin‐bound synthetic 15‐mer peptides and modified ELISAs by testing serum antibodies from patients and healthy donors. The serum antibodies of the healthy individuals did not show any specific recognition. Not only conformational but also linear epitope regions are spread in the entire extracellular region of the desmoglein 1 protein.
<blockFixed type="graphic"><mediaResourceGroup><mediaResource alt="image" href="urn:x-wiley:10752617:media:psc2476:psc2476-toc-0001"></mediaResource></mediaResourceGroup></blockFixed></p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>The mapping of linear B‐cell epitope regions in the extracellular parts of the desmoglein 1 and 3 proteins: recognition of immobilized peptides by pemphigus patients' serum autoantibodies</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>LINEAR B‐CELL EPITOPE REGIONS IN DESMOGLEIN 1 AND 3 PROTEINS</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>The mapping of linear B‐cell epitope regions in the extracellular parts of the desmoglein 1 and 3 proteins: recognition of immobilized peptides by pemphigus patients' serum autoantibodies</title></titleInfo><name type="personal"><namePart type="given">Hajnalka</namePart><namePart type="family">Szabados</namePart><affiliation>Research Group of Peptide Chemistry, Hungarian Academy of Sciences, Eötvös L. University, Budapest 112, PO Box 32 H‐1518, Hungary</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Szilvia</namePart><namePart type="family">Bősze</namePart><affiliation>Research Group of Peptide Chemistry, Hungarian Academy of Sciences, Eötvös L. University, Budapest 112, PO Box 32 H‐1518, Hungary</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Pálma</namePart><namePart type="family">Silló</namePart><affiliation>Department of Dermatology, Venereology and Dermato‐Oncology, Semmelweis University, Budapest, Hungary</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sarolta</namePart><namePart type="family">Kárpáti</namePart><affiliation>Department of Dermatology, Venereology and Dermato‐Oncology, Semmelweis University, Budapest, Hungary</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ferenc</namePart><namePart type="family">Hudecz</namePart><affiliation>Research Group of Peptide Chemistry, Hungarian Academy of Sciences, Eötvös L. University, Budapest 112, PO Box 32 H‐1518, Hungary</affiliation><affiliation>Institute of Chemistry, Eötvös L. University, Budapest, Hungary</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Katalin</namePart><namePart type="family">Uray</namePart><affiliation>Research Group of Peptide Chemistry, Hungarian Academy of Sciences, Eötvös L. University, Budapest 112, PO Box 32 H‐1518, Hungary</affiliation><affiliation>E-mail: uray@elte.hu</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><dateIssued encoding="w3cdtf">2013-02</dateIssued><dateCreated encoding="w3cdtf">2012-12-10</dateCreated><dateCaptured encoding="w3cdtf">2012-06-27</dateCaptured><dateValid encoding="w3cdtf">2012-11-19</dateValid><copyrightDate encoding="w3cdtf">2013</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract>Desmosomal transmembrane glycoproteins desmogleins (Dsg) 1 and 3 are targets of life‐threatening autoimmune blistering disorders such as Pemphigus vulgaris (PV) and Pemphigus foliaceus (PF). In these diseases, pemphigus autoantibodies are produced against Dsg1 and Dsg3 proteins. The autoantibodies bind to these transmembrane elements leading to a loss of desmosomal cell–cell adhesion and clinically, to the presence of blisters and erosions. Identification, characterization, and detailed analysis of the binding sites of autoantibodies have an outstanding importance in understanding the immunopathology of the disease and also in the design of novel diagnostics. Here, we describe the localization of the B‐cell epitope regions of Dsg1 and Dsg3 proteins' extracellular parts recognized by IgG‐type serum autoantibodies of patients with PV and PF. In our study, overlapping pentadecapeptides were synthesized on hydroxypropyl methacrylate pins based on the results of in silico predictions. To detect the interaction between the serum autoantibodies and the immobilized synthetic peptides, modified Enzyme Linked Immunosorbent Assay (ELISA) was performed with pin‐attached peptides testing the serum samples of ten patients and four healthy donors. We identified five possible epitope regions (aa86‐110, aa196‐220, aa226‐250, aa326‐340, and aa486‐520) within the extracellular part of the Dsg1 and four possible epitope regions (aa64‐78, aa330‐344, aa375‐399, and aa446‐460) within that of the Dsg3 protein sequence using these methods. Our data showed that serum autoantibodies of patients, previously identified as Dsg1 and Dsg3 positive, are able to recognize continuous linear epitope regions of both Dsg1 and Dsg3 proteins using pin‐bound overlapping peptides in modified ELISAs. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.</abstract><abstract type="graphical">Pemphigus specific epitope regions were identified in desmoglein 1 and 3 proteins with pin‐bound synthetic 15‐mer peptides and modified ELISAs by testing serum antibodies from patients and healthy donors. The serum antibodies of the healthy individuals did not show any specific recognition. Not only conformational but also linear epitope regions are spread in the entire extracellular region of the desmoglein 1 protein.</abstract><subject><genre>keywords</genre><topic>autoantibody epitopes</topic><topic>pin‐bound peptides</topic><topic>modified ELISA</topic><topic>desmoglein 1 and 3</topic><topic>pemphigus</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Peptide Science</title></titleInfo><titleInfo type="abbreviated"><title>J. Pept. Sci.</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><subject><genre>article-category</genre><topic>Research Article</topic><topic>Research Articles</topic></subject><identifier type="ISSN">1075-2617</identifier><identifier type="eISSN">1099-1387</identifier><identifier type="DOI">10.1002/(ISSN)1099-1387</identifier><identifier type="PublisherID">PSC</identifier><part><date>2013</date><detail type="volume"><caption>vol.</caption><number>19</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>84</start><end>94</end><total>11</total></extent></part></relatedItem><relatedItem type="references" displayLabel="psc2476-cit-0001"><titleInfo><title>Desmosomal cadherins: another growing multigene family of adhesion molecules</title></titleInfo><name type="personal"><namePart type="given">PJ</namePart><namePart type="family">Koch</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">WW</namePart><namePart type="family">Franke</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Koch PJ, Franke WW. 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