The recently discovered peptide editor TAPBPR binds to UDP-glucose:glycoprotein glucosyltransferase 1 to provide quality control in the antigen presentation pathway by facilitating the reglucosylation of the glycan on MHC class I molecules.
Temporal availability of antigen presentation by dendritic cells influences the differentiation of follicular helper T (Tfh) cells, which enhances germinal centre responses and induces protective immunity.
Tumor immunogenicity is quantified with a novel method, and the resulting tumor immunogenicity score is an effective tumor-inherent biomarker for prediction of response to immune checkpoint inhibitors.
Immunopeptidomics in combination with novel cell-based assays that assess peptide exchange reveal a critical role for the K22-D35 loop of TAPBPR in mediating peptide dissociation and peptide selection on MHC I.
Rodent herpesvirus Peru overcomes NK ‘missing-self’ killing using a non-classical MHC-I like protein resistant todownregulation by its own ubiquitin ligase that potently sabotages antigen presentation to T-cells.