Dataset for: Metabolite assignment of Ultra-Filtered Synovial Fluid extracted from knee joints of Reactive Arthritis patients using High-Resolution NMR spectroscopy

Currently, there are no reliable clinical biomarkers available that can aid early differential diagnosis of reactive arthritis (ReA) from other inflammatory joint diseases. Metabolic profiling of synovial fluid (SF) –obtained from joints affected in ReA- holds great promise in this regard and will further aid monitoring treatment and improving our understanding about disease mechanism. As a first step in this direction, we report here the metabolite specific assignment of 1H and 13C resonances detected in the NMR spectra of SF samples extracted from human patients with established ReA. The metabolite characterization has been carried out on both normal as well as on ultra-filtered (deproteinized) SF samples of eight ReA patients (n=8) using high resolution (800 MHz) 1H and 1H-13C NMR spectroscopy methods such as one-dimensional (1D) 1H CPMG and two-dimensional (2D) J-resolved1H NMR and homonuclear 1H-1H TOCSY and heteronuclear1H-13C HSQC correlation spectra. Compared to normal SF samples, several distinctive 1H NMR signals were identified and assigned to metabolites in the 1H NMR spectra of ultra-filtered SF samples. Overall, we assigned 53 metabolites in normal filtered SF and 64 metabolites in filtered pooled SF sample compared to normal (un-filtered) SF samples for which only 48 metabolites (including lipid/membrane metabolites as well) have been identified. The established NMR characterization of SF metabolites will serve to guide future metabolomics studies aiming to identify/evaluate the SF based metabolic biomarkers of diagnostic/prognostic potential or seeking biochemical insights into disease mechanisms in a clinical perspective

Dataset for: NMR Elucidation of Monomer-dimer transition and Conformational heterogeneity in Histone-like DNA binding protein of <i>Helicobacter pylori</i> (Hup)

<i>Helicobacter pylori</i> (<i>H. pylori</i>) colonizes under harsh acidic/oxidative stress conditions of human gastrointestinal tract and can survive there for infinitely longer durations of host life. The bacterium expresses several harbinger proteins to facilitate its persistent colonization under such conditions. One such protein in <i>H. pylori</i> is Histone like DNA binding protein (Hup) which in its homo-dimeric form binds to DNA to perform various DNA dependent cellular activities. Further, it also plays an important role in protecting the genomic DNA from oxidative stress and acidic denaturation. Legitimately, if the binding of Hup to DNA is suppressed, it will directly impact on the survival of the bacterium, thus making Hup a potential therapeutic target for developing new anti-<i>H. pylori</i> agents. However, to inhibit the binding of Hup to DNA, it is necessary to gain detailed insights into the molecular and structural basis of Hup-dimerization and its binding mechanism to DNA. As a first step in this direction, we report here the NMR assignments and structural features of Hup at pH of 6.0. The study revealed the occurrence of dynamic equilibrium between its monomer and dimer conformations. The dynamic equilibrium was found shifting towards dimer both at low temperature and pH; whereas DNA binding studies evidenced that the protein binds to DNA in its dimeric form. These preliminary investigations correlate very well with the diverse functionality of protein and will form the basis for future studies aiming to develop novel anti-<i>H. pylori</i> agents employing structure-based-rational drug discovery approach