{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T18:55:27Z","timestamp":1777575327712,"version":"3.51.4"},"reference-count":30,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2023,1,13]],"date-time":"2023-01-13T00:00:00Z","timestamp":1673568000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2023,7]]},"abstract":"<jats:p>Multiple sclerosis (MS) is an inflammatory and autoimmune disorder, in which an antibody\u2010mediated demyelination mechanism plays a critical role. We prepared two glucosylated peptides derived from the human myelin proteins, that is, oligodendrocyte\u2010myelin glycoprotein (OMGp) and reticulon\u20104 receptor (RTN4R), selected by a bioinformatic approach for their conformational homology with CSF114(Glc), a designed \u03b2\u2010turn antigenic probe derived from myelin oligodendrocyte glycoprotein (MOG), a glycoprotein present in the CNS. This synthetic antigen is specifically recognized by antibodies in sera of MS patients. We report herein the antigenic properties of these peptides, showing, on the one hand, that MS patient antibodies recognize the two glucosylated peptides and, on the other hand, that these antibodies cross\u2010react with CSF114(Glc) and with the previously described hyperglucosylated nontypeable <jats:styled-content style=\"fixed-case\"><jats:italic>Haemophilus influenzae<\/jats:italic><\/jats:styled-content> bacterial adhesin protein HMW1ct(Glc). These observations point to an immunological association between human and bacterial protein antigens, underpinning the hypothesis that molecular mimicry triggers the breakdown of self\u2010tolerance in MS and suggesting that RTN4R and OMGp can be considered as autoantigens.<\/jats:p>","DOI":"10.1002\/psc.3475","type":"journal-article","created":{"date-parts":[[2023,1,4]],"date-time":"2023-01-04T07:13:47Z","timestamp":1672816427000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Glucopeptides derived from myelin\u2010relevant proteins and hyperglucosylated nontypeable <scp><i>Haemophilus influenzae<\/i><\/scp> bacterial adhesin cross\u2010react with multiple sclerosis specific antibodies: A step forward in the identification of native autoantigens in multiple sclerosis"],"prefix":"10.1002","volume":"29","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0891-3405","authenticated-orcid":false,"given":"Michael","family":"Quagliata","sequence":"first","affiliation":[{"name":"Interdepartmental Research Unit of Peptide and Protein Chemistry and Biology, Department of Chemistry \u201cUgo Schiff\u201d University of Florence  Sesto Fiorentino Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Francesca","family":"Nuti","sequence":"additional","affiliation":[{"name":"Interdepartmental Research Unit of Peptide and Protein Chemistry and Biology, Department of Chemistry \u201cUgo Schiff\u201d University of Florence  Sesto Fiorentino Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5747-2285","authenticated-orcid":false,"given":"Feliciana","family":"Real\u2010Fernandez","sequence":"additional","affiliation":[{"name":"Institute of Chemistry of Organometallic Compounds (ICCOM) 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