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10.1038/s41467-020-16567-0 http://scihub22266oqcxt.onion/10.1038/s41467-020-16567-0 32461612!7253482!32461612     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2020 ; 11 (1): 2688 Nephropedia Template TP {{tp|p=32461612|t=2020. Vulnerabilities in coronavirus glycan shields despite extensive glycosylation |pdf=|usr=}}{{32461612}} gab.com Text Vulnerabilities in coronavirus glycan shields despite extensive glycosylation JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32461612 #FOAvip Severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoVs) are zoonotic pathogens with high fatality rates and pandemic potential. Vaccine development focuses on the principal target of the neutralizing humoral immune response, the spike (S) glycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66-87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a comparison of the global glycan density of coronavirus spikes with other viral proteins including HIV-1 envelope, Lassa virus glycoprotein complex, and influenza hemagglutinin, where glycosylation plays a known role in shielding immunogenic epitopes. Overall, our data reveal how organisation of glycosylation across class I viral fusion proteins influence not only individual glycan compositions but also the immunological pressure across the protein surface. Twit Text FOAVip Vulnerabilities in coronavirus glycan shields despite extensive glycosylation ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32461612 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32461612 #FOAvip English Wikipedia <ref>{{Cite pmid|32461612}}</ref> Vulnerabilities in coronavirus glycan shields despite extensive glycosylation #MMPMID32461612 Watanabe Y; Berndsen ZT; Raghwani J; Seabright GE; Allen JD; Pybus OG; McLellan JS; Wilson IA; Bowden TA; Ward AB; Crispin M Nat Commun 2020[May]; 11 (1): 2688 PMID32461612show ga Severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoVs) are zoonotic pathogens with high fatality rates and pandemic potential. Vaccine development focuses on the principal target of the neutralizing humoral immune response, the spike (S) glycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66-87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a comparison of the global glycan density of coronavirus spikes with other viral proteins including HIV-1 envelope, Lassa virus glycoprotein complex, and influenza hemagglutinin, where glycosylation plays a known role in shielding immunogenic epitopes. Overall, our data reveal how organisation of glycosylation across class I viral fusion proteins influence not only individual glycan compositions but also the immunological pressure across the protein surface. |*Middle East Respiratory Syndrome Coronavirus/immunology/metabolism[MESH] |*Polysaccharides/chemistry/immunology[MESH] |Coronavirus Infections/immunology/virology[MESH] |Cryoelectron Microscopy[MESH] |Epitopes/chemistry/immunology/metabolism[MESH] |Glycoproteins/chemistry/*immunology/ultrastructure[MESH] |Glycosylation[MESH] |HEK293 Cells[MESH] |HIV-1/immunology/metabolism[MESH] |Humans[MESH] |Immune Evasion/physiology[MESH] |Lassa virus/immunology/metabolism[MESH] |Orthomyxoviridae/immunology/metabolism[MESH] |Spike Glycoprotein, Coronavirus/chemistry/*immunology/ultrastructure[MESH] |Viral Fusion Proteins/chemistry/*immunology/ultrastructure[MESH]Vulnerabilities in coronavirus glycan shields despite extensive glycos(epmc).pdf DeepDyve Pubget Overpricing