Journal Article

PUBDB-2022-07175

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Opening opportunities for Kd determination and screening of MHC peptide complexes

Kopicki, J.-D.CSSB* ; Saikia, A. ; Niebling, S.CFEL*Extern*EMBL* ; Guenther, C.Extern* ; Anjanappa, R. ; Garcia-Alai, M. ; Springer, S. (Corresponding author) ; Uetrecht, C. (Corresponding author)CSSB*XFEL.EU*

2022
Springer Nature London

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Please use a persistent id in citations: doi:10.1038/s42003-022-03366-0  doi:10.3204/PUBDB-2022-07175

Abstract: An essential element of adaptive immunity is selective binding of peptide antigens by major histocompatibility complex (MHC) class I proteins and their presentation to cytotoxic T lymphocytes. Using native mass spectrometry, we analyze the binding of peptides to an empty disulfide-stabilized HLA-A*02:01 molecule and, due to its unique stability, we determine binding affinities of complexes loaded with truncated or charge-reduced peptides. We find that the two anchor positions can be stabilized independently, and we further analyze the contribution of additional amino acid positions to the binding strength. As a complement to computational prediction tools, our method estimates binding strength of even low-affinity peptides to MHC class I complexes quickly and efficiently. It has huge potential to eliminate binding affinity biases and thus accelerate drug discovery in infectious diseases, autoimmunity, vaccine design, and cancer immunotherapy.

Note: Deutsche Forschungsgemeinschaft grant SP583/12-1

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Contributing Institute(s):

1. CSSB - Leibniz-Institut für Experimentelle Virologie (LIV) / DESY - Charlotte Uetrecht (CSSB-LIV/DESY-CU)
2. The European XFEL Users (XFEL-User)

Research Program(s):

1. 899 - ohne Topic (POF4-899) (POF4-899)

Experiment(s):

1. No specific instrument

Appears in the scientific report 2022

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