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Structure and function of the non-classical major histocompatibility complex molecule MR1

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Abstract

Polymorphic major histocompatibility complex (MHC) molecules play a central role in the vertebrate adaptive immune system. By presenting short peptides derived from pathogen-derived proteins, these “classical” MHC molecules can alert the T cell branch of the immune system of infected cells and clear the pathogen. There exist other “non-classical” MHC molecules, which while similar in structure to classical MHC proteins, are contrasted by their limited polymorphism. While the functions of many class Ib MHC molecules have still to be elucidated, the nature and diversity of antigens (if any) that some of them might present to the immune system is expected to be more restricted and might function as another approach to distinguish self from non-self. The MHC-related 1 (MR1) molecule is a member of this family of non-classical MHC proteins. It was recently shown to present unique antigens in the form of vitamin metabolites found in certain microbes. MR1 is strongly conserved genetically, structurally, and functionally through mammalian evolution, indicating its necessity in ensuring an effective immune system for members of this class. Although MR1 will be celebrating 21 years this year since its discovery, most of our understanding of how this molecule functions has only been uncovered in the past decade. Herein, we discuss where MR1 is expressed, how it selectively is able to bind to its appropriate antigens and how it, then, is able to specifically activate a distinct population of T cells.

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Acknowledgments

Research in the Gapin’s laboratory is supported by National Institute of Health grant (AI103736). We would like to acknowledge current and past members of the laboratory for discussions and Drs. Jennifer Matsuda and Manfred Brigl for critical reading of the manuscript. We apologize to colleagues whose works were not cited due to space constraints or omission.

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  1. Department of Immunology and Microbiology, University of Colorado Anschutz Medical Campus, 12800 E. 19th Ave., Aurora, CO, USA

    S. Harsha Krovi & Laurent Gapin

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  1. S. Harsha Krovi
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Correspondence to Laurent Gapin.

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This article is published in the Special Issue CD1, MR1, NKT, and MAIT: Evolution and Origins of Non-peptidic Antigen Recognition by T lymphocytes with Guest Editor Dr. Dirk Zajonc

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Krovi, S.H., Gapin, L. Structure and function of the non-classical major histocompatibility complex molecule MR1. Immunogenetics 68, 549–559 (2016). https://doi.org/10.1007/s00251-016-0939-5

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