Crystal structure of the N-myristoylated lipopeptide-bound MHC class I complex

Daisuke Morita, Yukie Yamamoto, Tatsuaki Mizutani, Takeshi Ishikawa, Juri Suzuki, Tatsuhiko Igarashi, Naoki Mori, Takashi Shiina, Hidetoshi Inoko, Hiroaki Fujita, Kazuhiro Iwai, Yoshimasa Tanaka, Bunzo Mikami and Masahiko Sugita ()
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Daisuke Morita: Laboratory of Cell Regulation, Institute for Virus Research, Kyoto University
Yukie Yamamoto: Laboratory of Cell Regulation, Institute for Virus Research, Kyoto University
Tatsuaki Mizutani: Laboratory of Cell Regulation, Institute for Virus Research, Kyoto University
Takeshi Ishikawa: Graduate School of Biomedical Sciences, Nagasaki University
Juri Suzuki: Center for Human Evolution Modeling Research, Primate Research Institute, Kyoto University
Tatsuhiko Igarashi: Center for Emerging Virus Research, Institute for Virus Research, Kyoto University
Naoki Mori: Laboratory of Chemical Ecology, Graduate School of Agriculture, Kyoto University
Takashi Shiina: Tokai University School of Medicine
Hidetoshi Inoko: Tokai University School of Medicine
Hiroaki Fujita: Graduate School of Medicine, Kyoto University
Kazuhiro Iwai: Graduate School of Medicine, Kyoto University
Yoshimasa Tanaka: Center for Bioinformatics and Molecular Medicine, Graduate School of Biomedical Sciences, Nagasaki University
Bunzo Mikami: Laboratory of Applied Structural Biology, Graduate School of Agriculture, Kyoto University
Masahiko Sugita: Laboratory of Cell Regulation, Institute for Virus Research, Kyoto University

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: Abstract The covalent conjugation of a 14-carbon saturated fatty acid (myristic acid) to the amino-terminal glycine residue is critical for some viral proteins to function. This protein lipidation modification, termed N-myristoylation, is targeted by host cytotoxic T lymphocytes (CTLs) that specifically recognize N-myristoylated short peptides; however, the molecular mechanisms underlying lipopeptide antigen (Ag) presentation remain elusive. Here we show that a primate major histocompatibility complex (MHC) class I-encoded protein is capable of binding N-myristoylated 5-mer peptides and presenting them to specific CTLs. A high-resolution X-ray crystallographic analysis of the MHC class I:lipopeptide complex reveals an Ag-binding groove that is elaborately constructed to bind N-myristoylated short peptides rather than prototypic 9-mer peptides. The identification of lipopeptide-specific, MHC class I-restricted CTLs indicates that the widely accepted concept of MHC class I-mediated presentation of long peptides to CTLs may need some modifications to incorporate a novel MHC class I function of lipopeptide Ag presentation.

Date: 2016
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DOI: 10.1038/ncomms10356

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