Improved implant position and lower revision rate with robotic-assisted unicompartmental knee arthroplasty

PURPOSE: The aim of this case-control study was to compare implant position and revision rate for UKA, performed with either a robotic-assisted system or with conventional technique. METHODS: Eighty UKA (57 medial, 23 lateral) were performed with robotic assistance (BlueBelt Navio system) between 2013 and 2017. These patients were matched with 80 patients undergoing UKA using the same prosthesis, implanted using conventional technique. The sagittal and coronal component position was assessed on postoperative radiographs. The revision rate was reported at last follow-up. RESULTS: The mean follow-up was 19.7 months ±?9 for the robotic-assisted group, and 24.2 months ±?16 for the control group. The rate of postoperative limb alignment outliers (±?2°) was significantly higher in the control group than in the robotic-assisted group for both lateral UKA (26% in robotic group versus 61% in control group; p?=?0.018) and medial UKA (16% versus 32%, resp.; p?=?0.038). The coronal and sagittal tibial baseplate position had significantly less outliers (±?3°) in the robotic-assisted group, than in the control group. Revision rates were: 5% (n?=?4/80) for robotic assisted UKA and 9% (n?=?7/80) for conventional UKA (n.s.). The reasons for revision were different between groups, with 86% of revisions in the control group occurring in association with component malposition or limb malalignment, compared with none in the robotic-assisted group. CONCLUSION: Robotic-assisted UKA has a lower rate of postoperative limb alignment outliers, as well as a lower revision rate, compared to conventional technique. The accuracy of implant positioning is improved by this robotic-assisted system. LEVEL OF EVIDENCE: Level of evidence III. Retrospective case-control study CLINICAL RELEVANCE: This is the first paper comparing implant position, clinical outcome, and revision rate for UKA performed using the Navio robotic system with a control group

The Brucella TIR domain containing proteins BtpA and BtpB have a structural WxxxE motif important for protection against microtubule depolymerisation

BACKGROUND: The TIR domain-containing proteins BtpA/Btp1/TcpB and BtpB are translocated into host cells by the facultative intracellular bacterial pathogen Brucella. Here, they interfere with Toll like receptor signalling to temper the host inflammatory response. BtpA has also been found to modulate microtubule dynamics. In both proteins we identified a WxxxE motif, previously shown to be an essential structural component in a family of bacterial type III secretion system effectors that modulate host actin dynamics by functioning as guanine nucleotide exchange factors of host GTPases. We analysed a role for the WxxxE motif in association of BtpA and BtpB with the cytoskeleton. RESULTS: Unlike BtpA, ectopically expressed BtpB did not show a tubular localisation, but was found ubiquitously in the cytoplasm and the nucleus, and often appeared in discrete punctae in HeLa cells. BtpB was able to protect microtubules from drug-induced destabilisation similar to BtpA. The WxxxE motif was important for the ability of BtpA and BtpB to protect microtubules against destabilising drugs. Surprisingly, ectopic expression of BtpA, although not BtpB, in HeLa cells induced the formation of filopodia. This process was invariably dependent of the WxxxE motif. Our recent resolution of the crystal structure of the BtpA TIR domain reveals that the motif positions a glycine residue that has previously been shown to be essential for interaction of BtpA with microtubules. CONCLUSIONS: Our results suggest a structural role for the WxxxE motif in the association of BtpA and BtpB with microtubules, as with the WxxxE GEF family proteins where the motif positions an adjacent catalytic loop important for interaction with specific Rho GTPases. In addition, the ability of ectopically expressed BtpA to induce filopodia in a WxxxE-dependent manner suggests a novel property for BtpA. A conserved WxxxE motif is found in most bacterial and several eukaryotic TIR domain proteins. Despite the similarity between ectopically expressed BtpA and WxxxE GEFs to modulate host actin dynamics, our results suggest that BtpA is not part of this WxxxE GEF family. The WxxxE motif may therefore be a more common structural motif than thus far described. BtpA may provide clues to cross-talk between the TLR and GTPase signalling pathways. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12964-014-0053-y) contains supplementary material, which is available to authorized users

Amplitude of pancreatic lipase lid opening in solution and identification of spin label conformational subensembles by combining continuous wave and pulsed EPR spectroscopy and molecular dynamics.

International audienceThe opening of the lid that controls the access to the active site of human pancreatic lipase (HPL) was measured from the magnetic interaction between two spin labels grafted on this enzyme. One spin label was introduced at a rigid position in HPL where an accessible cysteine residue (C181) naturally occurs. A second spin label was covalently bound to the mobile lid after introducing a cysteine residue at position 249 by site-directed mutagenesis. Double electron-electron resonance (DEER) experiments allowed the estimation of a distance of 19 +/- 2 A between the spin labels when bilabeled HPL was alone in a frozen solution, i.e., with the lid in the closed conformation. A magnetic interaction was however detected by continuous wave EPR experiments, suggesting that a fraction of bilabeled HPL contained spin labels separated by a shorter distance. These results could be interpreted by the presence of two conformational subensembles for the spin label lateral chain at position 249 when the lid was closed. The existence of these conformational subensembles was revealed by molecular dynamics experiments and confirmed by the simulation of the EPR spectrum. When the lid opening was induced by the addition of bile salts and colipase, a larger distance of 43 +/- 2 A between the two spin labels was estimated from DEER experiments. The distances measured between the spin labels grafted at positions 181 and 249 were in good agreement with those estimated from the known X-ray structures of HPL in the closed and open conformations, but for the first time, the amplitude of the lid opening was measured in solution or in a frozen solution in the presence of amphiphiles