Visualising tapasin- and TAPBPR-assisted editing of major histocompatibility complex class-I immunopeptidomes
Visualising tapasin- and TAPBPR-assisted editing of major histocompatibility complex class-I immunopeptidomes
Which peptides are selected for presentation by major histocompatibility complex class-I (MHC-I) molecules is a key determinant of successful immune responses. Peptide selection is co-ordinated by the tapasin and TAP Binding
PRotein (TAPBPR) proteins, which ensure MHC-I molecules preferentially acquire high-affinity-binding peptides. New structural analyses have offered insight into how tapasin achieves this function within the peptide-loading complex (PLC)
(comprising the Transporter associated with Antigen Presentation (TAP) peptide transporter, tapasin–ERp57, MHC-I and calreticulin), and how TAPBPR performs a peptide editing function independently of other molecules. The new structures reveal nuances in how tapasin and TAPBPR interact with MHC-I, and how calreticulin and ERp57 complement tapasin to exploit the plasticity of MHC-I molecules to achieve peptide editing.
van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Elliott, Tim
b501b34d-da33-4866-84c0-2fdcb1809c77
August 2023
van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Elliott, Tim
b501b34d-da33-4866-84c0-2fdcb1809c77
van Hateren, Andy and Elliott, Tim
(2023)
Visualising tapasin- and TAPBPR-assisted editing of major histocompatibility complex class-I immunopeptidomes.
Current Opinion in Immunology, 83, [102340].
(doi:10.1016/j.coi.2023.102340).
Abstract
Which peptides are selected for presentation by major histocompatibility complex class-I (MHC-I) molecules is a key determinant of successful immune responses. Peptide selection is co-ordinated by the tapasin and TAP Binding
PRotein (TAPBPR) proteins, which ensure MHC-I molecules preferentially acquire high-affinity-binding peptides. New structural analyses have offered insight into how tapasin achieves this function within the peptide-loading complex (PLC)
(comprising the Transporter associated with Antigen Presentation (TAP) peptide transporter, tapasin–ERp57, MHC-I and calreticulin), and how TAPBPR performs a peptide editing function independently of other molecules. The new structures reveal nuances in how tapasin and TAPBPR interact with MHC-I, and how calreticulin and ERp57 complement tapasin to exploit the plasticity of MHC-I molecules to achieve peptide editing.
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e-pub ahead of print date: 26 May 2023
Published date: August 2023
Additional Information:
Funding Information:
The authors thank Rachel Darley for help with the figures. This work was supported by Cancer Research UK Program award A28279 awarded to TE. The authors declare that they have no conflicts of interest.
Publisher Copyright:
© 2023 The Authors
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Local EPrints ID: 477877
URI: http://eprints.soton.ac.uk/id/eprint/477877
ISSN: 0952-7915
PURE UUID: 703d1f7e-49aa-461e-a887-ff5764088638
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Date deposited: 15 Jun 2023 17:01
Last modified: 17 Mar 2024 03:08
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Tim Elliott
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