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10.1126/sciadv.abg7607 http://scihub22266oqcxt.onion/10.1126/sciadv.abg7607 33888467!8163077!33888467     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Adv 2021 ; 7 (22): ä Nephropedia Template TP {{tp|p=33888467|t=2021. SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity |pdf=|usr=}}{{33888467}} gab.com Text SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity JO: Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=33888467 #FOAvip The coronaviral spike is the dominant viral antigen and the target of neutralizing antibodies. We show that SARS-CoV-2 spike binds biliverdin and bilirubin, the tetrapyrrole products of heme metabolism, with nanomolar affinity. Using cryo-electron microscopy and x-ray crystallography, we mapped the tetrapyrrole interaction pocket to a deep cleft on the spike N-terminal domain (NTD). At physiological concentrations, biliverdin significantly dampened the reactivity of SARS-CoV-2 spike with immune sera and inhibited a subset of neutralizing antibodies. Access to the tetrapyrrole-sensitive epitope is gated by a flexible loop on the distal face of the NTD. Accompanied by profound conformational changes in the NTD, antibody binding requires relocation of the gating loop, which folds into the cleft vacated by the metabolite. Our results indicate that SARS-CoV-2 spike NTD harbors a dominant epitope, access to which can be controlled by an allosteric mechanism that is regulated through recruitment of a metabolite. Twit Text FOAVip SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity ????Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=33888467 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33888467 #FOAvip English Wikipedia <ref>{{Cite pmid|33888467}}</ref> SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity #MMPMID33888467 Rosa A; Pye VE; Graham C; Muir L; Seow J; Ng KW; Cook NJ; Rees-Spear C; Parker E; Dos Santos MS; Rosadas C; Susana A; Rhys H; Nans A; Masino L; Roustan C; Christodoulou E; Ulferts R; Wrobel AG; Short CE; Fertleman M; Sanders RW; Heaney J; Spyer M; Kjaer S; Riddell A; Malim MH; Beale R; MacRae JI; Taylor GP; Nastouli E; van Gils MJ; Rosenthal PB; Pizzato M; McClure MO; Tedder RS; Kassiotis G; McCoy LE; Doores KJ; Cherepanov P Sci Adv 2021[May]; 7 (22): ä PMID33888467show ga The coronaviral spike is the dominant viral antigen and the target of neutralizing antibodies. We show that SARS-CoV-2 spike binds biliverdin and bilirubin, the tetrapyrrole products of heme metabolism, with nanomolar affinity. Using cryo-electron microscopy and x-ray crystallography, we mapped the tetrapyrrole interaction pocket to a deep cleft on the spike N-terminal domain (NTD). At physiological concentrations, biliverdin significantly dampened the reactivity of SARS-CoV-2 spike with immune sera and inhibited a subset of neutralizing antibodies. Access to the tetrapyrrole-sensitive epitope is gated by a flexible loop on the distal face of the NTD. Accompanied by profound conformational changes in the NTD, antibody binding requires relocation of the gating loop, which folds into the cleft vacated by the metabolite. Our results indicate that SARS-CoV-2 spike NTD harbors a dominant epitope, access to which can be controlled by an allosteric mechanism that is regulated through recruitment of a metabolite. |Antibodies, Monoclonal/immunology/metabolism[MESH] |Antibodies, Neutralizing/immunology[MESH] |Bilirubin/metabolism[MESH] |Biliverdine/metabolism[MESH] |COVID-19/*immunology[MESH] |Cryoelectron Microscopy[MESH] |Crystallography, X-Ray[MESH] |Epitopes[MESH] |Heme/*metabolism[MESH] |Humans[MESH] |Immune Sera[MESH] |SARS-CoV-2/immunology/pathogenicity[MESH]SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity (epmc).pdf DeepDyve Pubget Overpricing