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IMMUNOLOGY

Chaperoning the dance of antigen presentation

Nature Chemical Biology volume 18, pages 796–797 (2022)Cite this article

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Antigen loading onto class I major histocompatibility complex (MHC-I) proteins relies on chaperones and protein flexibility. Researchers now provide new insight into the process, especially for the intriguing ‘non-classical’ MHC-I protein MR1, with implications for fundamental immunology and the development of novel immunotherapies.

Major histocompatibility complex (MHC) proteins are central players in immunity. This large group of proteins is responsible for presenting antigens to T cells, using a well-recognized architecture consisting of an antigen-binding groove formed by two α helices over a β-sheet floor. The classical class I proteins (referred to as MHC-I, or as the HLA-A, HLA-B and HLA-C proteins in humans) present short peptides derived from endogenously produced proteins. MHC-I proteins on the surface of a virus-infected cell, for example, will present peptides derived from intracellularly produced viral proteins. These flag the cell as infected and lead to its destruction when recognized by T cell receptors on cytotoxic T cells. Similar processes also occur during immune responses to cancer, where the presentation of peptides that incorporate mutations or reflect cellular dysfunction can also lead to destruction by T cells.

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Fig. 1: Differences in the dynamics of empty MHC-I and MR1 proteins alter recognition by TAPBPR.

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Authors and Affiliations

  1. Department of Chemistry & Biochemistry and the Harper Cancer Research Institute, University of Notre Dame, Notre Dame, IN, USA

    Tatiana J. Rosales & Brian M. Baker

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  1. Tatiana J. Rosales
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  2. Brian M. Baker
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Correspondence to Brian M. Baker.

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The authors declare no competing interests.

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Rosales, T.J., Baker, B.M. Chaperoning the dance of antigen presentation. Nat Chem Biol 18, 796–797 (2022). https://doi.org/10.1038/s41589-022-01069-5

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