<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-06-14T03:51:44Z</responseDate><request verb="GetRecord" identifier="oai:repisalud.isciii.es:20.500.12105/9694" metadataPrefix="marc">https://repisalud.isciii.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:repisalud.isciii.es:20.500.12105/9694</identifier><datestamp>2025-06-09T15:01:37Z</datestamp><setSpec>com_20.500.12105_2052</setSpec><setSpec>com_20.500.12105_2051</setSpec><setSpec>col_20.500.12105_19609</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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      <subfield code="a">Infantes, Susana</subfield>
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      <subfield code="a">Lorente, Elena</subfield>
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      <subfield code="a">Barnea, Eilon</subfield>
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      <subfield code="a">Beer, Ilan</subfield>
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      <subfield code="a">Barriga, Alejandro</subfield>
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      <subfield code="a">Lasala, Fátima</subfield>
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      <subfield code="a">Jimenez, Mercedes</subfield>
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      <subfield code="a">Admon, Arie</subfield>
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      <subfield code="a">Lopez, Daniel</subfield>
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      <subfield code="c">2013-04-12</subfield>
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      <subfield code="a">The presentation of short viral peptide antigens by human leukocyte antigen (HLA) class I molecules on cell surfaces is a key step in the activation of cytotoxic T lymphocytes, which mediate the killing of pathogen-infected cells or initiate autoimmune tissue damage. HLA-B27 is a well known class I molecule that is used to study both facets of the cellular immune response. Using mass spectrometry analysis of complex HLA-bound peptide pools isolated from large amounts of HLA-B*2705(+) cells, we identified 200 naturally processed HLA-B*2705 ligands. Our analyses revealed that a change in the position (P) 2 anchor motif was detected in the 3% of HLA-B*2705 ligands identified. B*2705 class I molecules were able to bind these six GlnP2 peptides, which showed significant homology to pathogenic bacterial sequences, with a broad range of affinities. One of these ligands was able to bind with distinct conformations to HLA-B27 subtypes differentially associated with ankylosing spondylitis. These conformational differences could be sufficient to initiate autoimmune damage in patients with ankylosing spondylitis-associated subtypes. Therefore, these kinds of peptides (short, with GlnP2, and similar low affinity to all HLA-B27 subtypes tested but with unlike conformations in differentially ankylosing spondylitis-associated subtypes) must not be excluded from future researches involving potential arthritogenic peptides.</subfield>
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      <subfield code="a">J Biol Chem  . 2013 Apr 12;288(15):10882-9.</subfield>
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      <subfield code="a">10.1074/jbc.M113.455352</subfield>
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      <subfield code="a">1083-351X</subfield>
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      <subfield code="a">0021-9258</subfield>
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      <subfield code="a">The Journal of biological chemistry</subfield>
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      <subfield code="a">23430249</subfield>
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      <subfield code="a">http://hdl.handle.net/20.500.12105/9694</subfield>
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      <subfield code="a">Natural HLA-B*2705 protein ligands with glutamine as anchor motif: implications for HLA-B27 association with spondyloarthropathy</subfield>
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