Publications by authors named "N M Lissin"

For effective targeted therapy of cancer with chemotherapy-loaded nanoparticles (NPs), antigens that are selective for cancer cells should be targeted to minimise off-tumour toxicity. Human leukocyte antigens (HLAs) are attractive cancer targets as they can present peptides from tumour-selective proteins on the cell surface, which can be recognised by T cells T cell receptors (TCRs). In this study, docetaxel-loaded polymeric NPs were conjugated to recombinant affinity-enhanced TCRs to target breast cancer cells presenting a tumour-selective peptide-HLA complex.

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Article Synopsis
  • Tumor-associated peptide-human leukocyte antigen complexes (pHLAs) are key targets for cancer therapies due to their role as cancer-specific epitopes on cell surfaces.
  • Two strategies are being developed to redirect T cells against these targets: using affinity-enhanced T cell receptors (ImmTACs) and TCR-mimic antibodies.
  • Research indicates that ImmTAC molecules have better selectivity and less off-target activity compared to TCR-mimic antibodies, which tend to bind more broadly, highlighting the importance of understanding pHLA specificity in designing effective cancer treatments.
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Tuberculosis (TB), caused by , remains a major human pandemic. Germline-encoded mycolyl lipid-reactive (GEM) T cells are donor-unrestricted and recognize CD1b-presented mycobacterial mycolates. However, the molecular requirements governing mycolate antigenicity for the GEM T cell receptor (TCR) remain poorly understood.

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The antiviral effects of hepatitis C virus (HCV)-specific CD8 T cells have been shown in an HCV replicon system but not in an authentic infectious HCV cell culture (HCVcc) system. Here, we developed tools to examine the antigenicity of HCV-infected HLA-A2-positive Huh7.5 hepatoma cells (Huh7.

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Cluster of differentiation 1c (CD1c)-dependent self-reactive T cells are abundant in human blood, but self-antigens presented by CD1c to the T-cell receptors of these cells are poorly understood. Here we present a crystal structure of CD1c determined at 2.4 Å revealing an extended ligand binding potential of the antigen groove and a substantially different conformation compared with known CD1c structures.

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