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, Immunoprecipitations were performed using 4 ?g of mouse monoclonal anti-Flag or rabbit polyclonal anti-NEU1 pre-adsorbed on protein G sepharose beads (GE Healthcare) for 2 h at 4 °C. Immunoprecipitated proteins were eluted with Laemmli buffer and subjected to SDS-PAGE and immunoblotting. Immunoblottings were performed using the indicated antibodies and immunoreactivity was revealed using a HRP-conjugated secondary antibodies (1/10,000) followed by enhanced chemiluminescence detection reagents and visualized with the Odyssey Fc LI-COR scanner
After sonication, crude membranes were pelleted by centrifugation at 20,000 g during 45 min at 4 °C and resuspended in 20 mM MES, pH4.5. Sialidase activity was assessed using the 2?-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid (BioSynth) as substrate. Assays were performed in triplicate (each run in duplicate) with 50 ?g of crude membranes proteins and 200 ?M of substrate for 2 h at 37 °C. Reactions were stopped by adding 1 M Na 2 CO 3 and the fluorescence of each well was measured in triplicate using an Infinite F200 PRO microplate reader (TECAN), Split-ubiquitin yeast two hybrid. The NEU1 cDNA was subcloned into pDONR221 before integration in the Split-Ubiquitin destination vectors. The Split-Ubiquitin vectors, pMetYC-DEST and pNX35-DEST, were used to produce the Met-repressible bait construct NEU1-Cub-PLV and prey construct NEU1-NubG, respectively. NubWT fragment, pMetYC-DEST and pNX35-DEST vectors were kindly provided by Dr F. Chaumont (Institut des Sciences de la Vie ,
, NEU1 homology model generation. Prediction of the human NEU1 3D structure was done by homology modeling using the SWISS-MODEL software 59-61 (accessible via the ExPASy web server) and the human NEU2 crystal structure
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