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Thermal Stability of Heterotrimeric pMHC Proteins as Determined by Circular Dichroism Spectroscopy.

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.

SUBMITTER: Fuller A

PROVIDER: S-EPMC5524174 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature

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Thermal Stability of Heterotrimeric pMHC Proteins as Determined by Circular Dichroism Spectroscopy.

Fuller Anna A Wall Aaron A Crowther Michael D MD Lloyd Angharad A Zhurov Alexei A Sewell Andrew K AK Cole David K DK Beck Konrad K

Bio-protocol 20170701 13

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 protec ...[more]

PMID: 28748203

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