{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,4]],"date-time":"2026-07-04T01:50:12Z","timestamp":1783129812398,"version":"3.54.6"},"reference-count":142,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2019,5,9]],"date-time":"2019-05-09T00:00:00Z","timestamp":1557360000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antibodies"],"abstract":"<jats:p>Monoclonal antibodies (mAbs) are valuable as research reagents, in diagnosis and in therapy. Their high specificity, the ease in production, favorable biophysical properties and the opportunity to engineer different properties make mAbs a versatile class of biologics. mAbs targeting peptide\u2013major histocompatibility molecule (pMHC) complexes are often referred to as \u201cTCR-like\u201d mAbs, as pMHC complexes are generally recognized by T-cell receptors (TCRs). Presentation of self- and non-self-derived peptide fragments on MHC molecules and subsequent activation of T cells dictate immune responses in health and disease. This includes responses to infectious agents or cancer but also aberrant responses against harmless self-peptides in autoimmune diseases. The ability of TCR-like mAbs to target specific peptides presented on MHC allows for their use to study peptide presentation or for diagnosis and therapy. This extends the scope of conventional mAbs, which are generally limited to cell-surface or soluble antigens. Herein, we review the strategies used to generate TCR-like mAbs and provide a structural comparison with the analogous TCR in pMHC binding. We further discuss their applications as research tools and therapeutic reagents in preclinical models as well as challenges and limitations associated with their use.<\/jats:p>","DOI":"10.3390\/antib8020032","type":"journal-article","created":{"date-parts":[[2019,5,9]],"date-time":"2019-05-09T11:22:35Z","timestamp":1557400955000},"page":"32","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":48,"title":["Targeting the MHC Ligandome by Use of TCR-Like Antibodies"],"prefix":"10.3390","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6070-1413","authenticated-orcid":false,"given":"Lene St\u00f8kken","family":"H\u00f8ydahl","sequence":"first","affiliation":[{"name":"Department of Immunology, University of Oslo and Oslo University Hospital, N-0372 Oslo, Norway"},{"name":"KG Jebsen Coeliac Disease Research Centre, University of Oslo, N-0372 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rahel","family":"Frick","sequence":"additional","affiliation":[{"name":"Department of Immunology, University of Oslo and Oslo University Hospital, N-0372 Oslo, Norway"},{"name":"Department of Biosciences, University of Oslo, N-0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Inger","family":"Sandlie","sequence":"additional","affiliation":[{"name":"Department of Immunology, University of Oslo and Oslo University Hospital, N-0372 Oslo, Norway"},{"name":"Department of Biosciences, University of Oslo, N-0316 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5257-8571","authenticated-orcid":false,"given":"Geir \u00c5ge","family":"L\u00f8set","sequence":"additional","affiliation":[{"name":"Department of Biosciences, University of Oslo, N-0316 Oslo, Norway"},{"name":"Nextera AS, N-0349 Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,5,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/s41577-018-0007-5","article-title":"Understanding the drivers of mhc restriction of t cell receptors","volume":"18","author":"Gras","year":"2018","journal-title":"Nat. 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