Citation link: http://dx.doi.org/10.25819/ubsi/10249
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Dokument Type: Article
metadata.dc.title: Opening opportunities for Kd determination and screening of MHC peptide complexes
Authors: Kopicki, Janine-Denise 
Saikia, Ankur 
Niebling, Stephan 
Günther, Christian 
Anjanappa, Raghavendra 
Garcia-Alai, Maria 
Springer, Sebastian 
Uetrecht, Charlotte 
Institute: Fakultät V - Lebenswissenschaftliche Fakultät 
Free keywords: High-throughput screening, Mass spectrometry, MHC class I, Molecular biophysics
Dewey Decimal Classification: 610 Medizin, Gesundheit
GHBS-Clases: VVL
UUI
UXA
Issue Date: 2022
Publish Date: 2023
Source: Communications biology ; 5, article number 488. - https://doi.org/10.1038/s42003-022-03366-0
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.
Description: 
Finanziert im Rahmen der DEAL-Verträge durch die Universitätsbibliothek Siegen
DOI: http://dx.doi.org/10.25819/ubsi/10249
URN: urn:nbn:de:hbz:467-24432
URI: https://dspace.ub.uni-siegen.de/handle/ubsi/2443
License: http://creativecommons.org/licenses/by/4.0/
Appears in Collections:Geförderte Open-Access-Publikationen

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