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10.1126/science.abe6230 http://scihub22266oqcxt.onion/10.1126/science.abe6230 33436526!7932109!33436526     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2021 ; 371 (6530): ä Nephropedia Template TP {{tp|p=33436526|t=2021. Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape |pdf=|usr=}}{{33436526}} gab.com Text Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=33436526 #FOAvip The pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to spread, with devastating consequences. For passive immunization efforts, nanobodies have size and cost advantages over conventional antibodies. In this study, we generated four neutralizing nanobodies that target the receptor binding domain of the SARS-CoV-2 spike protein. We used x-ray crystallography and cryo-electron microscopy to define two distinct binding epitopes. On the basis of these structures, we engineered multivalent nanobodies with more than 100 times the neutralizing activity of monovalent nanobodies. Biparatopic nanobody fusions suppressed the emergence of escape mutants. Several nanobody constructs neutralized through receptor binding competition, whereas other monovalent and biparatopic nanobodies triggered aberrant activation of the spike fusion machinery. These premature conformational changes in the spike protein forestalled productive fusion and rendered the virions noninfectious. Twit Text FOAVip Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape ????Science http://www.kidney.de/pget.php?&tw=1&pmid=33436526 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33436526 #FOAvip English Wikipedia <ref>{{Cite pmid|33436526}}</ref> Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape #MMPMID33436526 Koenig PA; Das H; Liu H; Kummerer BM; Gohr FN; Jenster LM; Schiffelers LDJ; Tesfamariam YM; Uchima M; Wuerth JD; Gatterdam K; Ruetalo N; Christensen MH; Fandrey CI; Normann S; Todtmann JMP; Pritzl S; Hanke L; Boos J; Yuan M; Zhu X; Schmid-Burgk JL; Kato H; Schindler M; Wilson IA; Geyer M; Ludwig KU; Hallberg BM; Wu NC; Schmidt FI Science 2021[Feb]; 371 (6530): ä PMID33436526show ga The pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to spread, with devastating consequences. For passive immunization efforts, nanobodies have size and cost advantages over conventional antibodies. In this study, we generated four neutralizing nanobodies that target the receptor binding domain of the SARS-CoV-2 spike protein. We used x-ray crystallography and cryo-electron microscopy to define two distinct binding epitopes. On the basis of these structures, we engineered multivalent nanobodies with more than 100 times the neutralizing activity of monovalent nanobodies. Biparatopic nanobody fusions suppressed the emergence of escape mutants. Several nanobody constructs neutralized through receptor binding competition, whereas other monovalent and biparatopic nanobodies triggered aberrant activation of the spike fusion machinery. These premature conformational changes in the spike protein forestalled productive fusion and rendered the virions noninfectious. |Amino Acid Substitution[MESH] |Angiotensin-Converting Enzyme 2/metabolism[MESH] |Animals[MESH] |Antibodies, Neutralizing/chemistry/*immunology/metabolism[MESH] |Antibodies, Viral/chemistry/*immunology/metabolism[MESH] |Antibody Affinity[MESH] |Antigens, Viral/immunology[MESH] |Binding Sites, Antibody[MESH] |COVID-19/*immunology/virology[MESH] |Cell Line[MESH] |Cryoelectron Microscopy[MESH] |Epitopes[MESH] |Humans[MESH] |Membrane Fusion[MESH] |Mutation[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Receptors, Coronavirus/metabolism[MESH] |SARS-CoV-2/genetics/*immunology/physiology[MESH] |Single-Domain Antibodies/chemistry/*immunology/metabolism[MESH] |Spike Glycoprotein, Coronavirus/chemistry/genetics/*immunology/metabolism[MESH]Structure-guided multivalent nanobodies block SARS-CoV-2 infection and(epmc).pdf DeepDyve Pubget Overpricing