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10.15252/embj.2021108375 http://scihub22266oqcxt.onion/10.15252/embj.2021108375 34375000!8420505!34375000     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+J 2021 ; 40 (19): e108375 Nephropedia Template TP {{tp|p=34375000|t=2021. Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites |pdf=|usr=}}{{34375000}} gab.com Text Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=34375000 #FOAvip New SARS-CoV-2 variants are continuously emerging with critical implications for therapies or vaccinations. The 22 N-glycan sites of Spike remain highly conserved among SARS-CoV-2 variants, opening an avenue for robust therapeutic intervention. Here we used a comprehensive library of mammalian carbohydrate-binding proteins (lectins) to probe critical sugar residues on the full-length trimeric Spike and the receptor binding domain (RBD) of SARS-CoV-2. Two lectins, Clec4g and CD209c, were identified to strongly bind to Spike. Clec4g and CD209c binding to Spike was dissected and visualized in real time and at single-molecule resolution using atomic force microscopy. 3D modelling showed that both lectins can bind to a glycan within the RBD-ACE2 interface and thus interferes with Spike binding to cell surfaces. Importantly, Clec4g and CD209c significantly reduced SARS-CoV-2 infections. These data report the first extensive map and 3D structural modelling of lectin-Spike interactions and uncovers candidate receptors involved in Spike binding and SARS-CoV-2 infections. The capacity of CLEC4G and mCD209c lectins to block SARS-CoV-2 viral entry holds promise for pan-variant therapeutic interventions. Twit Text FOAVip Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=34375000 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34375000 #FOAvip English Wikipedia <ref>{{Cite pmid|34375000}}</ref> Identification of lectin receptors for conserved SARS-CoV-2 glycosylation sites #MMPMID34375000 Hoffmann D; Mereiter S; Jin Oh Y; Monteil V; Elder E; Zhu R; Canena D; Hain L; Laurent E; Grunwald-Gruber C; Klausberger M; Jonsson G; Kellner MJ; Novatchkova M; Ticevic M; Chabloz A; Wirnsberger G; Hagelkruys A; Altmann F; Mach L; Stadlmann J; Oostenbrink C; Mirazimi A; Hinterdorfer P; Penninger JM EMBO J 2021[Oct]; 40 (19): e108375 PMID34375000show ga New SARS-CoV-2 variants are continuously emerging with critical implications for therapies or vaccinations. The 22 N-glycan sites of Spike remain highly conserved among SARS-CoV-2 variants, opening an avenue for robust therapeutic intervention. Here we used a comprehensive library of mammalian carbohydrate-binding proteins (lectins) to probe critical sugar residues on the full-length trimeric Spike and the receptor binding domain (RBD) of SARS-CoV-2. Two lectins, Clec4g and CD209c, were identified to strongly bind to Spike. Clec4g and CD209c binding to Spike was dissected and visualized in real time and at single-molecule resolution using atomic force microscopy. 3D modelling showed that both lectins can bind to a glycan within the RBD-ACE2 interface and thus interferes with Spike binding to cell surfaces. Importantly, Clec4g and CD209c significantly reduced SARS-CoV-2 infections. These data report the first extensive map and 3D structural modelling of lectin-Spike interactions and uncovers candidate receptors involved in Spike binding and SARS-CoV-2 infections. The capacity of CLEC4G and mCD209c lectins to block SARS-CoV-2 viral entry holds promise for pan-variant therapeutic interventions. |Animals[MESH] |Binding Sites/physiology[MESH] |COVID-19/virology[MESH] |Cell Line[MESH] |Chlorocebus aethiops[MESH] |Glycosylation[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Mice[MESH] |Molecular Dynamics Simulation[MESH] |Protein Binding/physiology[MESH] |Receptors, Mitogen/*metabolism[MESH] |SARS-CoV-2/*metabolism[MESH] |Vero Cells[MESH]Identification of lectin receptors for conserved SARS-CoV-2 glycosylat(epmc).pdf DeepDyve Pubget Overpricing