4pg2
The crystal structure of H-2Db with a S-glutathionylated peptideThe crystal structure of H-2Db with a S-glutathionylated peptide
Structural highlights
FunctionHA11_MOUSE Involved in the presentation of foreign antigens to the immune system. Publication Abstract from PubMedCysteine-containing peptides represent an important class of T cell epitopes, yet their prevalence remains underestimated. We have established and interrogated a database of around 70,000 naturally processed MHC bound peptides and demonstrate that cysteine-containing peptides are presented on the surface of cells in an MHC allomorph dependent manner and comprise on average 5-10% of the immunopeptidome. A significant proportion of these peptides are oxidatively modified, most commonly through covalent linkage with the antioxidant glutathione. Unlike some of the previously reported Cysteine-based modifications, this represents a true physiological alteration of cysteine residues. Furthermore, our results suggest that alterations in the cellular redox state induced by viral infection are communicated to the immune system through the presentation of S-glutathionylated viral peptides, resulting in altered T cell recognition. Our data provide a structural basis for how the glutathione modification alters recognition by virus-specific T cells. Collectively, these results suggest that oxidative stress represents a mechanism for modulating the virus-specific T cell response. The Cellular Redox Environment Alters Antigen Presentation.,Trujillo JA, Croft NP, Dudek NL, Channappanavar R, Theodossis A, Webb AI, Dunstone MA, Illing PT, Butler NS, Fett C, Tscharke DC, Rossjohn J, Perlman S, Purcell AW J Biol Chem. 2014 Aug 18. pii: jbc.M114.573402. PMID:25135637[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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