4 research outputs found

    A European spine registry

    Get PDF
    Abstract.: New joint replacement registries are being widely implemented across national and international organizations. The need for a continuous long-term post-market surveillance of implants has been recognized, and has become increasingly important to ensure the quality of prosthetic components. Registry data with large case numbers represent an acceptable alternative to controlled randomized clinical trials, which are often difficult to conduct in orthopedic surgery. The variety of implants and procedures in spinal surgery not only induces the same need for long-term monitoring of post-surgical product performance as in the joint replacement subspecialties, but also renders essential the establishment of a comprehensive spine registry for all major pathologies and interventions. In cooperation with the M.E. Müller Institute for Evaluative Research in Orthopedic Surgery (MEM-CED) at the University of Berne, Switzerland, the Spine Society of Europe (SSE) has launched Spine Tango: the first modular and multilevel European online registry for spinal surgery. Within Spine Tango, the major challenge in registry design and structure is the definition of and agreement upon a core set of questions as a common European dataset. Additional questions for national or individual interest can also be dynamically added to the core dataset. An automated implant tracking system has also been setup, which allows highly precise product documentation without additional work for clinical staff member

    Characterization of a bacterial copper‐dependent lytic polysaccharide monooxygenase with an unusual second coordination sphere

    No full text
    International audienceLytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes involved in the degradation of recalcitrant polysaccharides such as cellulose or chitin. LPMOs act in synergy with glycoside hydrolases such as cellulases and chitinases by oxidatively cleaving a number of glycosidic bonds at the surface of their crystalline substrate(s). Besides their role in biomass degradation, some bacterial LPMOs have been found to be virulence factors in some human and insect pathogens. Photorhabdus luminescens is a nematode symbiont bacterium that is pathogenic to a wide range of insects. A single gene encoding a LPMO is found in its genome. In this work, we report the characterization of this LPMO, referred to as PlAA10. Surprisingly, PlAA10 lacks the conserved alanine residue (substituted by an isoleucine) found in the second coordination sphere of the copper-active site in bacterial LPMOs. PlAA10 was found to be catalytically active on both alpha- and beta-chitin, and exhibits a C1-oxidation regiospecificity, similarly to other chitin-active LPMOs. The 1.6 angstrom X-ray crystal structure confirmed that PlAA10 adopts the canonical immunoglobulin-like fold typical for LPMOs. The geometry of the copper-active site is not affected by the nearby isoleucine, as also supported by electron paramagnetic resonance. Nevertheless, the bulkier side chain of isoleucine protrudes from the substrate-binding surface. A bioinformatic study on putative bacterial LPMOs unveiled that they exhibit some variability at the conserved active-site alanine position with a substitution in about 15% of all sequences analyzed. Database Structural data (atomic coordinates and structure factors) reported for PlAA10 are available in the Protein Data Bank under accession number . Enzymes PlAA10,
    corecore