Project description:This study aimed to characterise the transcriptomic response of the lactate-utilizing bacteria, Coprococcus catus and Anaerobutyricum soehngenii, grown on varying carbon sources. This work has allowed for identification of divergent gene clusters in each species contributing to the lactate utilisation pathway.
Project description:Innate-like gd T effector subsets are exported from the thymus as “memory-like” cells prewired for rapid, specialized function. Previously, we showed that emergent gd subsets distinguished by TCRg and TCRd usage in the fetal and adult thymus possess distinct global transcriptomes and the subset-specific combinatorial expression of High Mobility Group box transcription factors (HMG TFs) shown as a primary determinant of gd effector differentiation. While the detailed mechanism of HMG TFs cooperativity and counter-regulations are not fully understood, a key feature for IL-17 producing gd T effectors (Tgd 17) is predicted to be context-dependent interactions between SOX13 and TCF1 that result in diversified target gene regulation. Assay for Transposase-Accessible Chromatin with high throughput sequencing (ATACseq) will map chromatin accessibility genome wide. Each read will provide information about the positions of nucleosomes and nucleosome-free regions.
Project description:The retention of galactose-deficient IgA1 (Gd-IgA1) in the glomerular mesangium is a hallmark of IgA nephropathy (IgAN). The immune complex formed by Gd-IgA1 binds to transferrin receptor 1 (TfR1) and deposits on mesangial cell, inducing cell proliferation, inflammatory response, matrix secretion, etc., causes organic damage and dysfunction of the kidney. Even though, the mechanism of how Gd-IgA1 recognize and bind to TfR1 is unclear. In this experiment, we ami to determine the specific interaction region responsible for Gd-IgA1 and TfR1. We prepared a complex of Gd-IgA1 and TfR1 by incubating the two proteins under acidic conditions and stabilizing it using the chemical cross-linking agent glutaraldehyde. And then, the gel bands corresponding to the Gd-IgA1-TfR1 complex was exexcised from the SDS-PAGE gel and analyzed by high-resolution mass spectrometry. This analysis identified fragments containing the hinge peptide sequence, with the R276 residue interacting with the E350 and D356 residues in the apical domain of TfR1. Our results reveal that the hinge peptide of Gd-IgA1 interacts specifically with the apical domain of TfR1.
