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10.3390/v14020317 http://scihub22266oqcxt.onion/10.3390/v14020317 35215911!8876212!35215911     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       Viruses 2022 ; 14 (2): ä Nephropedia Template TP {{tp|p=35215911|t=2022. Ferristatin II Efficiently Inhibits SARS-CoV-2 Replication in Vero Cells |pdf=|usr=}}{{35215911}} gab.com Text Ferristatin II Efficiently Inhibits SARS-CoV-2 Replication in Vero Cells JO: Viruses http://www.kidney.de/pget.php?&tw=1&pmid=35215911 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to have a significant impact on global public health. Multiple mechanisms for SARS-CoV-2 cell entry have been described; however, the role of transferrin receptor 1 (TfR1) in SARS-CoV-2 infection has received little attention. We used ferristatin II to induce the degradation of TfR1 on the surface of Vero cells and to study the consequences of such treatment on the viability of the cells and the replication of SARS-CoV-2. We demonstrated that ferristatin II is non-toxic for Vero cells in concentrations up to 400 microM. According to confocal microscopy data, the distribution of the labeled transferrin and receptor-binding domain (RBD) of Spike protein is significantly affected by the 18h pretreatment with 100 microM ferristatin II in culture medium. The uptake of RBD protein is nearly fully inhibited by ferristatin II treatment, although this protein remains bound on the cell surface. The findings were well confirmed by the significant inhibition of the SARS-CoV-2 infection of Vero cells by ferristatin II with IC(50) values of 27 microM (for Wuhan D614G virus) and 40 microM (for Delta virus). A significant reduction in the infectious titer of the Omicron SARS-CoV-2 variant was noted at a ferristatin II concentration as low as 6.25 microM. We hypothesize that ferristatin II blocks the TfR1-mediated SARS-CoV-2 host cell entry; however, further studies are needed to elucidate the full mechanisms of this virus inhibition, including the effect of ferristatin II on other SARS-CoV-2 receptors, such as ACE2, Neuropilin-1 and CD147. The inhibition of viral entry by targeting the receptor on the host cells, rather than the viral mutation-prone protein, is a promising COVID-19 therapeutic strategy. Twit Text FOAVip Ferristatin II Efficiently Inhibits SARS-CoV-2 Replication in Vero Cells ????Viruses http://www.kidney.de/pget.php?&tw=1&pmid=35215911 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35215911 #FOAvip English Wikipedia <ref>{{Cite pmid|35215911}}</ref> Ferristatin II Efficiently Inhibits SARS-CoV-2 Replication in Vero Cells #MMPMID35215911 Sokolov A; Isakova-Sivak I; Grudinina N; Mezhenskaya D; Litasova E; Kostevich V; Stepanova E; Rak A; Sychev I; Kirik O; Rudenko L Viruses 2022[Feb]; 14 (2): ä PMID35215911show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to have a significant impact on global public health. Multiple mechanisms for SARS-CoV-2 cell entry have been described; however, the role of transferrin receptor 1 (TfR1) in SARS-CoV-2 infection has received little attention. We used ferristatin II to induce the degradation of TfR1 on the surface of Vero cells and to study the consequences of such treatment on the viability of the cells and the replication of SARS-CoV-2. We demonstrated that ferristatin II is non-toxic for Vero cells in concentrations up to 400 microM. According to confocal microscopy data, the distribution of the labeled transferrin and receptor-binding domain (RBD) of Spike protein is significantly affected by the 18h pretreatment with 100 microM ferristatin II in culture medium. The uptake of RBD protein is nearly fully inhibited by ferristatin II treatment, although this protein remains bound on the cell surface. The findings were well confirmed by the significant inhibition of the SARS-CoV-2 infection of Vero cells by ferristatin II with IC(50) values of 27 microM (for Wuhan D614G virus) and 40 microM (for Delta virus). A significant reduction in the infectious titer of the Omicron SARS-CoV-2 variant was noted at a ferristatin II concentration as low as 6.25 microM. We hypothesize that ferristatin II blocks the TfR1-mediated SARS-CoV-2 host cell entry; however, further studies are needed to elucidate the full mechanisms of this virus inhibition, including the effect of ferristatin II on other SARS-CoV-2 receptors, such as ACE2, Neuropilin-1 and CD147. The inhibition of viral entry by targeting the receptor on the host cells, rather than the viral mutation-prone protein, is a promising COVID-19 therapeutic strategy. |Animals[MESH] |Biphenyl Compounds/*pharmacology[MESH] |Chlorocebus aethiops[MESH] |Inhibitory Concentration 50[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Receptors, Transferrin/antagonists & inhibitors[MESH] |SARS-CoV-2/*drug effects[MESH] |Sulfones/*pharmacology[MESH] |Vero Cells[MESH] |Virus Internalization/*drug effects[MESH]Ferristatin II Efficiently Inhibits SARS-CoV-2 Replication in Vero Cel(epmc).pdf DeepDyve Pubget Overpricing