Thermal stability of heterotrimeric pMHC proteins as determined by circular dichroism spectroscopy

Fuller, Anna, Wall, Aaron, Crowther, Michael D., Lloyd, Angharad, Zhurov, Alexei ORCID: https://orcid.org/0000-0002-5594-0740, Sewell, Andrew K. ORCID: https://orcid.org/0000-0003-3194-3135, Cole, David K. ORCID: https://orcid.org/0000-0003-0028-9396 and Beck, Konrad ORCID: https://orcid.org/0000-0001-5098-9484 2017. Thermal stability of heterotrimeric pMHC proteins as determined by circular dichroism spectroscopy. Bio-protocol 7 (13) , -. 10.21769/BioProtoc.2366

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Abstract

T cell receptor (TCR) recognition of foreign peptide fragments, presented by peptide major histocompatibility complex (pMHC), governs T-cell mediated protection against pathogens and cancer. Many factors govern T-cell sensitivity, including the affinity of the TCR-pMHC interaction and the stability of pMHC on the surface of antigen presenting cells. These factors are particularly relevant for the peptide vaccination field, in which more stable pMHC interactions could enable more effective protection against disease. Here, we discuss a method for the determination of pMHC stability that we have used to investigate HIV immune escape, T-cell sensitivity to cancer antigens and mechanisms leading to autoimmunity.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry Medicine
Publisher:	Bio-Protocol
ISSN:	2331-8325
Date of First Compliant Deposit:	1 August 2017
Last Modified:	05 Jan 2024 08:11
URI:	https://orca.cardiff.ac.uk/id/eprint/102133

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