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10.1016/j.jmb.2020.166748 http://scihub22266oqcxt.onion/10.1016/j.jmb.2020.166748 33310017!7833242!33310017     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Biol 2021 ; 433 (3): 166748 Nephropedia Template TP {{tp|p=33310017|t=2021. The ACE2-binding Interface of SARS-CoV-2 Spike Inherently Deflects Immune Recognition |pdf=|usr=}}{{33310017}} gab.com Text The ACE2-binding Interface of SARS-CoV-2 Spike Inherently Deflects Immune Recognition JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=33310017 #FOAvip The COVID-19 pandemic remains a global threat, and host immunity remains the main mechanism of protection against the disease. The spike protein on the surface of SARS-CoV-2 is a major antigen and its engagement with human ACE2 receptor plays an essential role in viral entry into host cells. Consequently, antibodies targeting the ACE2-interacting surface (ACE2IS) located in the receptor-binding domain (RBD) of the spike protein can neutralize the virus. However, the understanding of immune responses to SARS-CoV-2 is still limited, and it is unclear how the virus protects this surface from recognition by antibodies. Here, we designed an RBD mutant that disrupts the ACE2IS and used it to characterize the prevalence of antibodies directed to the ACE2IS from convalescent sera of 94 COVID-19-positive patients. We found that only a small fraction of RBD-binding antibodies targeted the ACE2IS. To assess the immunogenicity of different parts of the spike protein, we performed in vitro antibody selection for the spike and the RBD proteins using both unbiased and biased selection strategies. Intriguingly, unbiased selection yielded antibodies that predominantly targeted regions outside the ACE2IS, whereas ACE2IS-binding antibodies were readily identified from biased selection designed to enrich such antibodies. Furthermore, antibodies from an unbiased selection using the RBD preferentially bound to the surfaces that are inaccessible in the context of whole spike protein. These results suggest that the ACE2IS has evolved less immunogenic than the other regions of the spike protein, which has important implications in the development of vaccines against SARS-CoV-2. Twit Text FOAVip The ACE2-binding Interface of SARS-CoV-2 Spike Inherently Deflects Immune Recognition ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=33310017 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33310017 #FOAvip English Wikipedia <ref>{{Cite pmid|33310017}}</ref> The ACE2-binding Interface of SARS-CoV-2 Spike Inherently Deflects Immune Recognition #MMPMID33310017 Hattori T; Koide A; Noval MG; Panchenko T; Romero LA; Teng KW; Tada T; Landau NR; Stapleford KA; Koide S J Mol Biol 2021[Feb]; 433 (3): 166748 PMID33310017show ga The COVID-19 pandemic remains a global threat, and host immunity remains the main mechanism of protection against the disease. The spike protein on the surface of SARS-CoV-2 is a major antigen and its engagement with human ACE2 receptor plays an essential role in viral entry into host cells. Consequently, antibodies targeting the ACE2-interacting surface (ACE2IS) located in the receptor-binding domain (RBD) of the spike protein can neutralize the virus. However, the understanding of immune responses to SARS-CoV-2 is still limited, and it is unclear how the virus protects this surface from recognition by antibodies. Here, we designed an RBD mutant that disrupts the ACE2IS and used it to characterize the prevalence of antibodies directed to the ACE2IS from convalescent sera of 94 COVID-19-positive patients. We found that only a small fraction of RBD-binding antibodies targeted the ACE2IS. To assess the immunogenicity of different parts of the spike protein, we performed in vitro antibody selection for the spike and the RBD proteins using both unbiased and biased selection strategies. Intriguingly, unbiased selection yielded antibodies that predominantly targeted regions outside the ACE2IS, whereas ACE2IS-binding antibodies were readily identified from biased selection designed to enrich such antibodies. Furthermore, antibodies from an unbiased selection using the RBD preferentially bound to the surfaces that are inaccessible in the context of whole spike protein. These results suggest that the ACE2IS has evolved less immunogenic than the other regions of the spike protein, which has important implications in the development of vaccines against SARS-CoV-2. |A549 Cells[MESH] |Angiotensin-Converting Enzyme 2/genetics/*immunology/*metabolism[MESH] |Animals[MESH] |Antibodies, Neutralizing/immunology[MESH] |Antibodies, Viral/immunology[MESH] |Binding Sites[MESH] |Chlorocebus aethiops[MESH] |Epitopes/immunology[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Immune Sera[MESH] |Immunoglobulin G/metabolism[MESH] |Mutation[MESH] |Spike Glycoprotein, Coronavirus/genetics/*immunology/*metabolism[MESH]The ACE2-binding Interface of SARS-CoV-2 Spike Inherently Deflects Imm(epmc).pdf DeepDyve Pubget Overpricing