Review of the mathematical foundations of data fusion techniques in surface metrology

The recent proliferation of engineered surfaces, including freeform and structured surfaces, is challenging current metrology techniques. Measurement using multiple sensors has been proposed to achieve enhanced benefits, mainly in terms of spatial frequency bandwidth, which a single sensor cannot provide. When using data from different sensors, a process of data fusion is required and there is much active research in this area. In this paper, current data fusion methods and applications are reviewed, with a focus on the mathematical foundations of the subject. Common research questions in the fusion of surface metrology data are raised and potential fusion algorithms are discussed

A conserved energetic footprint underpins recognition of human leukocyte antigen-E by two distinct αβ T cell receptors

\u3b1\u3b2 T cell receptors (TCRs) interact with peptides bound to the polymorphic Major Histocompatibility Complex class Ia (MHC-Ia) and class II (MHC-II) molecules, as well as the essentially monomorphic MHC class Ib (MHC-Ib) molecules. While there is a large amount of information on how TCRs engage with MHC-Ia and MHC-II, our understanding of TCR-MHC-Ib interactions is very limited. Infection with cytomegalovirus (CMV) can elicit a CD8+ T cell response restricted by the human MHC-Ib molecule, Human Leukocyte Antigen (HLA)-E, and specific for an epitope from UL40 (VMAPRTLIL), which is characterized by biased TRBV14 gene usage. Here we describe an HLA-E-restricted CD8+ T cell able to recognize an allotypic variant of the UL40 peptide, with a modification at position 8 (P8) of the peptide (VMAPRTLVL) that uses the TRBV9 gene segment. We report the structures of a TRBV9+ TCR in complex with the HLA-E molecule presenting the two peptides. Our data revealed that the TRBV9+ TCR adopts a different docking mode and molecular footprint atop HLA-E when compared with the TRBV14+ TCR-HLA-E ternary complex. Additionally, despite their differing V gene segment usage and different docking mechanisms, mutational analyses showed that the TCRs shared a conserved energetic footprint on the HLA-E molecule, focussed around the peptide-binding groove. Hence, we provide new insights into how monomorphic MHC molecules interact with T cells