Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.cell.2021.05.032 http://scihub22266oqcxt.onion/10.1016/j.cell.2021.05.032 34139176!8142859!34139176     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 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       Cell 2021 ; 184 (13): 3452-3466.e18 Nephropedia Template TP {{tp|p=34139176|t=2021. An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies |pdf=|usr=}}{{34139176}} gab.com Text An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=34139176 #FOAvip Antibodies against the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein prevent SARS-CoV-2 infection. However, the effects of antibodies against other spike protein domains are largely unknown. Here, we screened a series of anti-spike monoclonal antibodies from coronavirus disease 2019 (COVID-19) patients and found that some of antibodies against the N-terminal domain (NTD) induced the open conformation of RBD and thus enhanced the binding capacity of the spike protein to ACE2 and infectivity of SARS-CoV-2. Mutational analysis revealed that all of the infectivity-enhancing antibodies recognized a specific site on the NTD. Structural analysis demonstrated that all infectivity-enhancing antibodies bound to NTD in a similar manner. The antibodies against this infectivity-enhancing site were detected at high levels in severe patients. Moreover, we identified antibodies against the infectivity-enhancing site in uninfected donors, albeit at a lower frequency. These findings demonstrate that not only neutralizing antibodies but also enhancing antibodies are produced during SARS-CoV-2 infection. Twit Text FOAVip An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=34139176 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34139176 #FOAvip English Wikipedia <ref>{{Cite pmid|34139176}}</ref> An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies #MMPMID34139176 Liu Y; Soh WT; Kishikawa JI; Hirose M; Nakayama EE; Li S; Sasai M; Suzuki T; Tada A; Arakawa A; Matsuoka S; Akamatsu K; Matsuda M; Ono C; Torii S; Kishida K; Jin H; Nakai W; Arase N; Nakagawa A; Matsumoto M; Nakazaki Y; Shindo Y; Kohyama M; Tomii K; Ohmura K; Ohshima S; Okamoto T; Yamamoto M; Nakagami H; Matsuura Y; Nakagawa A; Kato T; Okada M; Standley DM; Shioda T; Arase H Cell 2021[Jun]; 184 (13): 3452-3466.e18 PMID34139176show ga Antibodies against the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein prevent SARS-CoV-2 infection. However, the effects of antibodies against other spike protein domains are largely unknown. Here, we screened a series of anti-spike monoclonal antibodies from coronavirus disease 2019 (COVID-19) patients and found that some of antibodies against the N-terminal domain (NTD) induced the open conformation of RBD and thus enhanced the binding capacity of the spike protein to ACE2 and infectivity of SARS-CoV-2. Mutational analysis revealed that all of the infectivity-enhancing antibodies recognized a specific site on the NTD. Structural analysis demonstrated that all infectivity-enhancing antibodies bound to NTD in a similar manner. The antibodies against this infectivity-enhancing site were detected at high levels in severe patients. Moreover, we identified antibodies against the infectivity-enhancing site in uninfected donors, albeit at a lower frequency. These findings demonstrate that not only neutralizing antibodies but also enhancing antibodies are produced during SARS-CoV-2 infection. |Animals[MESH] |Antibodies, Monoclonal/*immunology[MESH] |Antibodies, Neutralizing/*immunology[MESH] |Antibodies, Viral/*immunology[MESH] |COVID-19/immunology[MESH] |Cell Line[MESH] |Chlorocebus aethiops[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Protein Binding/immunology[MESH] |Protein Domains/immunology[MESH] |SARS-CoV-2/*immunology[MESH] |Spike Glycoprotein, Coronavirus/genetics/*immunology[MESH]An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted(epmc).pdf DeepDyve Pubget Overpricing