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10.1016/j.antiviral.2020.104868 http://scihub22266oqcxt.onion/10.1016/j.antiviral.2020.104868 32659292!7351055!32659292     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 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Antiviral+Res 2020 ; 182 (ä): 104868 Nephropedia Template TP {{tp|p=32659292|t=2020. Immunoglobulin fragment F(ab )(2) against RBD potently neutralizes SARS-CoV-2 in vitro |pdf=|usr=}}{{32659292}} gab.com Text Immunoglobulin fragment F(ab )(2) against RBD potently neutralizes SARS-CoV-2 in vitro JO: Antiviral Res http://www.kidney.de/pget.php?&tw=1&pmid=32659292 #FOAvip COVID-19, which is caused by the emerging human coronavirus SARS-CoV-2, has become a global pandemic that poses a serious threat to human health. To date, no vaccines or specific antiviral drugs have been approved for the treatment of this disease in clinic. Herein, therapeutic antibodies for SARS-CoV-2 were obtained from hyperimmune equine plasma. First, a recombinant SARS-CoV-2 spike protein receptor-binding domain (RBD) was obtained in gram-level quantities through high-cell density fermentation of Chinese hamster ovary cells. Then, the binding of the RBD to the SARS-CoV-2 receptor, human angiotensin-converting enzyme 2, was verified by several biochemical methods. The efficacy of the RBD in triggering antibody response in vivo was subsequently tested in both mice and equines, and the results showed that the RBD triggered high-titer neutralizing antibody production in vivo. Immunoglobulin F(ab')(2) fragments were prepared from equine antisera via removal of the Fc region from the immunoglobulins. Finally, a neutralization test with live virus demonstrated that RBD-specific F(ab')(2) inhibited SARS-CoV-2 with an EC(50) of 0.07 mug/ml and an EC(80) of 0.18 mug/ml, showing a potent inhibitory effect on SARS-CoV-2. These results highlight RBD-specific equine immunoglobulin F(ab')(2) fragment as a candidate for the treatment of SARS-CoV-2. Twit Text FOAVip Immunoglobulin fragment F(ab )(2) against RBD potently neutralizes SARS-CoV-2 in vitro ????Antiviral Res http://www.kidney.de/pget.php?&tw=1&pmid=32659292 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32659292 #FOAvip English Wikipedia <ref>{{Cite pmid|32659292}}</ref> Immunoglobulin fragment F(ab )(2) against RBD potently neutralizes SARS-CoV-2 in vitro #MMPMID32659292 Pan X; Zhou P; Fan T; Wu Y; Zhang J; Shi X; Shang W; Fang L; Jiang X; Shi J; Sun Y; Zhao S; Gong R; Chen Z; Xiao G Antiviral Res 2020[Oct]; 182 (ä): 104868 PMID32659292show ga COVID-19, which is caused by the emerging human coronavirus SARS-CoV-2, has become a global pandemic that poses a serious threat to human health. To date, no vaccines or specific antiviral drugs have been approved for the treatment of this disease in clinic. Herein, therapeutic antibodies for SARS-CoV-2 were obtained from hyperimmune equine plasma. First, a recombinant SARS-CoV-2 spike protein receptor-binding domain (RBD) was obtained in gram-level quantities through high-cell density fermentation of Chinese hamster ovary cells. Then, the binding of the RBD to the SARS-CoV-2 receptor, human angiotensin-converting enzyme 2, was verified by several biochemical methods. The efficacy of the RBD in triggering antibody response in vivo was subsequently tested in both mice and equines, and the results showed that the RBD triggered high-titer neutralizing antibody production in vivo. Immunoglobulin F(ab')(2) fragments were prepared from equine antisera via removal of the Fc region from the immunoglobulins. Finally, a neutralization test with live virus demonstrated that RBD-specific F(ab')(2) inhibited SARS-CoV-2 with an EC(50) of 0.07 mug/ml and an EC(80) of 0.18 mug/ml, showing a potent inhibitory effect on SARS-CoV-2. These results highlight RBD-specific equine immunoglobulin F(ab')(2) fragment as a candidate for the treatment of SARS-CoV-2. |Animals[MESH] |Antibodies, Neutralizing/*immunology[MESH] |Antibodies, Viral/immunology[MESH] |Betacoronavirus/*immunology[MESH] |COVID-19[MESH] |Chlorocebus aethiops[MESH] |Coronavirus Infections/*therapy/*virology[MESH] |Female[MESH] |HeLa Cells[MESH] |Humans[MESH] |Mice, Inbred BALB C[MESH] |Neutralization Tests[MESH] |Pandemics[MESH] |Pneumonia, Viral/*therapy/*virology[MESH] |Protein Binding[MESH] |Receptors, Immunologic/*immunology[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/*immunology[MESH]Immunoglobulin fragment F(ab )(2) against RBD potently neutralizes SAR(epmc).pdf DeepDyve Pubget Overpricing