Allele-specific Alterations in the Peptidome Underlie the Joint Association of HLA-A*29:02 and Endoplasmic Reticulum Aminopeptidase 2 (ERAP2) with Birdshot Chorioretinopathy.
Identifieur interne : 000901 ( PubMed/Corpus ); précédent : 000900; suivant : 000902Allele-specific Alterations in the Peptidome Underlie the Joint Association of HLA-A*29:02 and Endoplasmic Reticulum Aminopeptidase 2 (ERAP2) with Birdshot Chorioretinopathy.
Auteurs : Alejandro Sanz-Bravo ; Adrian Martín-Esteban ; Jonas J W. Kuiper ; Marina García-Peydr ; Eilon Barnea ; Arie Admon ; José A. L Pez De CastroSource :
- Molecular & cellular proteomics : MCP [ 1535-9484 ] ; 2018.
English descriptors
- KwdEn :
- Alleles, Aminopeptidases (chemistry), Aminopeptidases (genetics), Aminopeptidases (metabolism), Birdshot Chorioretinopathy, Cell Line, Chorioretinitis (genetics), Genetic Predisposition to Disease, HLA-A Antigens (genetics), Humans, Hydrophobic and Hydrophilic Interactions, Ligands, Peptides (metabolism), Proteome (genetics).
- MESH :
- chemical , chemistry : Aminopeptidases.
- chemical , genetics : Aminopeptidases, HLA-A Antigens, Proteome.
- chemical , metabolism : Aminopeptidases, Peptides.
- genetics : Chorioretinitis.
- Alleles, Birdshot Chorioretinopathy, Cell Line, Genetic Predisposition to Disease, Humans, Hydrophobic and Hydrophilic Interactions, Ligands.
Abstract
Virtually all patients of the rare inflammatory eye disease birdshot chorioretinopathy (BSCR) carry the HLA-A*29:02 allele. BSCR is also associated with endoplasmic reticulum aminopeptidase 2 (ERAP2), an enzyme involved in processing HLA class I ligands, thus implicating the A*29:02 peptidome in this disease. To investigate the relationship between both risk factors we employed label-free quantitative mass spectrometry to characterize the effects of ERAP2 on the A*29:02-bound peptidome. An ERAP2-negative cell line was transduced with lentiviral constructs containing GFP-ERAP2 or GFP alone, and the A*29:02 peptidomes from both transduced cells were compared. A similar analysis was performed with two additional A*29:02-positive, ERAP1-concordant, cell lines expressing or not ERAP2. In both comparisons the presence of ERAP2 affected the following features of the A*29:02 peptidome: 1) Length, with increased amounts of peptides >9-mers, and 2) N-terminal residues, with less ERAP2-susceptible and more hydrophobic ones. The paradoxical effects on peptide length suggest that unproductive binding to ERAP2 might protect some peptides from ERAP1 over-trimming. The influence on N-terminal residues can be explained by a direct effect of ERAP2 on trimming, without ruling out and improved processing in concert with ERAP1. The alterations in the A*29:02 peptidome suggest that the association of ERAP2 with BSCR is through its effects on peptide processing. These differ from those on the ankylosing spondylitis-associated HLA-B*27. Thus, ERAP2 alters the peptidome of distinct HLA molecules as a function of their specific binding preferences, influencing different pathological outcomes in an allele-dependent way.
DOI: 10.1074/mcp.RA118.000778
PubMed: 29769354
Links to Exploration step
pubmed:29769354Le document en format XML
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Kuiper</name><affiliation><nlm:affiliation>§Department of Ophthalmology, University Medical Center Utrecht, The Netherlands.</nlm:affiliation></affiliation></author><author><name sortKey="Garcia Peydr, Marina" sort="Garcia Peydr, Marina" uniqKey="Garcia Peydr M" first="Marina" last="García-Peydr">Marina García-Peydr</name><affiliation><nlm:affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain.</nlm:affiliation></affiliation></author><author><name sortKey="Barnea, Eilon" sort="Barnea, Eilon" uniqKey="Barnea E" first="Eilon" last="Barnea">Eilon Barnea</name><affiliation><nlm:affiliation>¶Faculty of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel.</nlm:affiliation></affiliation></author><author><name sortKey="Admon, Arie" sort="Admon, Arie" uniqKey="Admon A" first="Arie" last="Admon">Arie Admon</name><affiliation><nlm:affiliation>¶Faculty of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel.</nlm:affiliation></affiliation></author><author><name sortKey="L Pez De Castro, Jose A" sort="L Pez De Castro, Jose A" uniqKey="L Pez De Castro J" first="José A" last="L Pez De Castro">José A. L Pez De Castro</name><affiliation><nlm:affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain; aldecastro@cbm.csic.es.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:29769354</idno><idno type="pmid">29769354</idno><idno type="doi">10.1074/mcp.RA118.000778</idno><idno type="wicri:Area/PubMed/Corpus">000901</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000901</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Allele-specific Alterations in the Peptidome Underlie the Joint Association of HLA-A*29:02 and Endoplasmic Reticulum Aminopeptidase 2 (ERAP2) with Birdshot Chorioretinopathy.</title><author><name sortKey="Sanz Bravo, Alejandro" sort="Sanz Bravo, Alejandro" uniqKey="Sanz Bravo A" first="Alejandro" last="Sanz-Bravo">Alejandro Sanz-Bravo</name><affiliation><nlm:affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain.</nlm:affiliation></affiliation></author><author><name sortKey="Martin Esteban, Adrian" sort="Martin Esteban, Adrian" uniqKey="Martin Esteban A" first="Adrian" last="Martín-Esteban">Adrian Martín-Esteban</name><affiliation><nlm:affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain.</nlm:affiliation></affiliation></author><author><name sortKey="Kuiper, Jonas J W" sort="Kuiper, Jonas J W" uniqKey="Kuiper J" first="Jonas J W" last="Kuiper">Jonas J W. Kuiper</name><affiliation><nlm:affiliation>§Department of Ophthalmology, University Medical Center Utrecht, The Netherlands.</nlm:affiliation></affiliation></author><author><name sortKey="Garcia Peydr, Marina" sort="Garcia Peydr, Marina" uniqKey="Garcia Peydr M" first="Marina" last="García-Peydr">Marina García-Peydr</name><affiliation><nlm:affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain.</nlm:affiliation></affiliation></author><author><name sortKey="Barnea, Eilon" sort="Barnea, Eilon" uniqKey="Barnea E" first="Eilon" last="Barnea">Eilon Barnea</name><affiliation><nlm:affiliation>¶Faculty of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel.</nlm:affiliation></affiliation></author><author><name sortKey="Admon, Arie" sort="Admon, Arie" uniqKey="Admon A" first="Arie" last="Admon">Arie Admon</name><affiliation><nlm:affiliation>¶Faculty of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel.</nlm:affiliation></affiliation></author><author><name sortKey="L Pez De Castro, Jose A" sort="L Pez De Castro, Jose A" uniqKey="L Pez De Castro J" first="José A" last="L Pez De Castro">José A. L Pez De Castro</name><affiliation><nlm:affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain; aldecastro@cbm.csic.es.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Molecular & cellular proteomics : MCP</title><idno type="eISSN">1535-9484</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alleles</term><term>Aminopeptidases (chemistry)</term><term>Aminopeptidases (genetics)</term><term>Aminopeptidases (metabolism)</term><term>Birdshot Chorioretinopathy</term><term>Cell Line</term><term>Chorioretinitis (genetics)</term><term>Genetic Predisposition to Disease</term><term>HLA-A Antigens (genetics)</term><term>Humans</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Ligands</term><term>Peptides (metabolism)</term><term>Proteome (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Aminopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Aminopeptidases</term><term>HLA-A Antigens</term><term>Proteome</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aminopeptidases</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Chorioretinitis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Alleles</term><term>Birdshot Chorioretinopathy</term><term>Cell Line</term><term>Genetic Predisposition to Disease</term><term>Humans</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Ligands</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Virtually all patients of the rare inflammatory eye disease birdshot chorioretinopathy (BSCR) carry the HLA-A*29:02 allele. BSCR is also associated with endoplasmic reticulum aminopeptidase 2 (ERAP2), an enzyme involved in processing HLA class I ligands, thus implicating the A*29:02 peptidome in this disease. To investigate the relationship between both risk factors we employed label-free quantitative mass spectrometry to characterize the effects of ERAP2 on the A*29:02-bound peptidome. An ERAP2-negative cell line was transduced with lentiviral constructs containing GFP-ERAP2 or GFP alone, and the A*29:02 peptidomes from both transduced cells were compared. A similar analysis was performed with two additional A*29:02-positive, ERAP1-concordant, cell lines expressing or not ERAP2. In both comparisons the presence of ERAP2 affected the following features of the A*29:02 peptidome: 1) Length, with increased amounts of peptides >9-mers, and 2) N-terminal residues, with less ERAP2-susceptible and more hydrophobic ones. The paradoxical effects on peptide length suggest that unproductive binding to ERAP2 might protect some peptides from ERAP1 over-trimming. The influence on N-terminal residues can be explained by a direct effect of ERAP2 on trimming, without ruling out and improved processing in concert with ERAP1. The alterations in the A*29:02 peptidome suggest that the association of ERAP2 with BSCR is through its effects on peptide processing. These differ from those on the ankylosing spondylitis-associated HLA-B*27. Thus, ERAP2 alters the peptidome of distinct HLA molecules as a function of their specific binding preferences, influencing different pathological outcomes in an allele-dependent way.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29769354</PMID><DateCompleted><Year>2019</Year><Month>04</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1535-9484</ISSN><JournalIssue CitedMedium="Internet"><Volume>17</Volume><Issue>8</Issue><PubDate><Year>2018</Year><Month>08</Month></PubDate></JournalIssue><Title>Molecular & cellular proteomics : MCP</Title><ISOAbbreviation>Mol. Cell Proteomics</ISOAbbreviation></Journal><ArticleTitle>Allele-specific Alterations in the Peptidome Underlie the Joint Association of HLA-A*29:02 and Endoplasmic Reticulum Aminopeptidase 2 (ERAP2) with Birdshot Chorioretinopathy.</ArticleTitle><Pagination><MedlinePgn>1564-1577</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/mcp.RA118.000778</ELocationID><Abstract><AbstractText>Virtually all patients of the rare inflammatory eye disease birdshot chorioretinopathy (BSCR) carry the HLA-A*29:02 allele. BSCR is also associated with endoplasmic reticulum aminopeptidase 2 (ERAP2), an enzyme involved in processing HLA class I ligands, thus implicating the A*29:02 peptidome in this disease. To investigate the relationship between both risk factors we employed label-free quantitative mass spectrometry to characterize the effects of ERAP2 on the A*29:02-bound peptidome. An ERAP2-negative cell line was transduced with lentiviral constructs containing GFP-ERAP2 or GFP alone, and the A*29:02 peptidomes from both transduced cells were compared. A similar analysis was performed with two additional A*29:02-positive, ERAP1-concordant, cell lines expressing or not ERAP2. In both comparisons the presence of ERAP2 affected the following features of the A*29:02 peptidome: 1) Length, with increased amounts of peptides >9-mers, and 2) N-terminal residues, with less ERAP2-susceptible and more hydrophobic ones. The paradoxical effects on peptide length suggest that unproductive binding to ERAP2 might protect some peptides from ERAP1 over-trimming. The influence on N-terminal residues can be explained by a direct effect of ERAP2 on trimming, without ruling out and improved processing in concert with ERAP1. The alterations in the A*29:02 peptidome suggest that the association of ERAP2 with BSCR is through its effects on peptide processing. These differ from those on the ankylosing spondylitis-associated HLA-B*27. Thus, ERAP2 alters the peptidome of distinct HLA molecules as a function of their specific binding preferences, influencing different pathological outcomes in an allele-dependent way.</AbstractText><CopyrightInformation>© 2018 Sanz-Bravo et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sanz-Bravo</LastName><ForeName>Alejandro</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martín-Esteban</LastName><ForeName>Adrian</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kuiper</LastName><ForeName>Jonas J W</ForeName><Initials>JJW</Initials><AffiliationInfo><Affiliation>§Department of Ophthalmology, University Medical Center Utrecht, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>García-Peydró</LastName><ForeName>Marina</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Barnea</LastName><ForeName>Eilon</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>¶Faculty of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Admon</LastName><ForeName>Arie</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>¶Faculty of Biology, Technion - Israel Institute of Technology, Haifa 32000, Israel.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>López de Castro</LastName><ForeName>José A</ForeName><Initials>JA</Initials><AffiliationInfo><Affiliation>From the ‡Centro de Biología Molecular Severo Ochoa (CSIC-UAM), 28049 Madrid, Spain; aldecastro@cbm.csic.es.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>05</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Cell Proteomics</MedlineTA><NlmUniqueID>101125647</NlmUniqueID><ISSNLinking>1535-9476</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015234">HLA-A Antigens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C035524">HLA-A29 antigen</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008024">Ligands</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020543">Proteome</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.11.-</RegistryNumber><NameOfSubstance UI="D000626">Aminopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.11.-</RegistryNumber><NameOfSubstance UI="C503944">ERAP2 protein, human</NameOfSubstance></Chemical></ChemicalList><SupplMeshList><SupplMeshName Type="Disease" UI="C537630">Birdshot chorioretinopathy</SupplMeshName></SupplMeshList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000483" MajorTopicYN="Y">Alleles</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000626" MajorTopicYN="N">Aminopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000080365" MajorTopicYN="N">Birdshot Chorioretinopathy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002825" MajorTopicYN="N">Chorioretinitis</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020022" MajorTopicYN="Y">Genetic Predisposition to Disease</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015234" MajorTopicYN="N">HLA-A Antigens</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057927" MajorTopicYN="N">Hydrophobic and Hydrophilic Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008024" MajorTopicYN="N">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020543" MajorTopicYN="N">Proteome</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Antigen processing</Keyword><Keyword MajorTopicYN="Y">Birdshot chorioretinopathy</Keyword><Keyword MajorTopicYN="Y">ERAP2</Keyword><Keyword MajorTopicYN="Y">Enzymes</Keyword><Keyword MajorTopicYN="Y">HLA-A*29:02</Keyword><Keyword MajorTopicYN="Y">Immunology</Keyword><Keyword MajorTopicYN="Y">Inflammation</Keyword><Keyword MajorTopicYN="Y">Mass Spectrometry</Keyword><Keyword 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