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Most of these modified peptides are captured in the <jats:styled-content style=\"fixed-case\">MHC<\/jats:styled-content> class I groove in a similar manner to that for unmodified peptides. <jats:italic>N<\/jats:italic>\u2010Myristoylated 5\u2010mer lipopeptides have recently been identified as a novel chemical class of <jats:styled-content style=\"fixed-case\">MHC<\/jats:styled-content> class I\u2010presented antigens. The rhesus classical <jats:styled-content style=\"fixed-case\">MHC<\/jats:styled-content> class I allele, Mamu\u2010B*098, was found to be capable of binding <jats:italic>N<\/jats:italic>\u2010myristoylated lipopeptides and presenting them to <jats:styled-content style=\"fixed-case\">CTL<\/jats:styled-content>s. A high\u2010resolution X\u2010ray crystallographic analysis of the Mamu\u2010B*098:lipopeptide complex revealed that the myristic group as well as conserved C\u2010terminal serine residue of the lipopeptide ligand functioned as anchors, whereas the short stretch of three amino acid residues located in the middle of the lipopeptides was only exposed externally with the potential to interact directly with specific T\u2010cell receptors. Therefore, the modes of lipopeptide\u2013ligand interactions with <jats:styled-content style=\"fixed-case\">MHC<\/jats:styled-content> class I and with T\u2010cell receptors are novel and fundamentally distinct from that for <jats:styled-content style=\"fixed-case\">MHC<\/jats:styled-content> class I\u2010presented peptides. Another lipopeptide\u2010presenting <jats:styled-content style=\"fixed-case\">MHC<\/jats:styled-content> class I allele has now been identified, leading us to the prediction that <jats:styled-content style=\"fixed-case\">MHC<\/jats:styled-content> class I molecules may be separated on a functional basis into two groups: one presenting long peptides and the other presenting short lipopeptides. Since the <jats:italic>N<\/jats:italic>\u2010myristoylation of viral proteins is often linked to pathogenesis, <jats:styled-content style=\"fixed-case\">CTL<\/jats:styled-content>s capable of sensing <jats:italic>N<\/jats:italic>\u2010myristoylation may serve to control pathogenic viruses, raising the possibility for the development of a new type of lipopeptide vaccine.<\/jats:p>","DOI":"10.1111\/imm.12646","type":"journal-article","created":{"date-parts":[[2016,7,12]],"date-time":"2016-07-12T08:22:45Z","timestamp":1468311765000},"page":"139-145","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Lipopeptides: a novel antigen repertoire presented by major histocompatibility complex class I molecules"],"prefix":"10.1111","volume":"149","author":[{"given":"Daisuke","family":"Morita","sequence":"first","affiliation":[{"name":"Laboratory of Cell Regulation Institute for Virus Research Kyoto University Kyoto 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