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10.1038/s41598-020-72528-z http://scihub22266oqcxt.onion/10.1038/s41598-020-72528-z 32985513!7522990!32985513     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2020 ; 10 (1): 15917 Nephropedia Template TP {{tp|p=32985513|t=2020. Structural and functional modelling of SARS-CoV-2 entry in animal models |pdf=|usr=}}{{32985513}} gab.com Text Structural and functional modelling of SARS-CoV-2 entry in animal models JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=32985513 #FOAvip SARS-CoV-2 is the novel coronavirus responsible for the outbreak of COVID-19, a disease that has spread to over 100 countries and, as of the 26th July 2020, has infected over 16 million people. Despite the urgent need to find effective therapeutics, research on SARS-CoV-2 has been affected by a lack of suitable animal models. To facilitate the development of medical approaches and novel treatments, we compared the ACE2 receptor, and TMPRSS2 and Furin proteases usage of the SARS-CoV-2 Spike glycoprotein in human and in a panel of animal models, i.e. guinea pig, dog, cat, rat, rabbit, ferret, mouse, hamster and macaque. Here we showed that ACE2, but not TMPRSS2 or Furin, has a higher level of sequence variability in the Spike protein interaction surface, which greatly influences Spike protein binding mode. Using molecular docking simulations we compared the SARS-CoV and SARS-CoV-2 Spike proteins in complex with the ACE2 receptor and showed that the SARS-CoV-2 Spike glycoprotein is compatible to bind the human ACE2 with high specificity. In contrast, TMPRSS2 and Furin are sufficiently similar in the considered hosts not to drive susceptibility differences. Computational analysis of binding modes and protein contacts indicates that macaque, ferrets and hamster are the most suitable models for the study of inhibitory antibodies and small molecules targeting the SARS-CoV-2 Spike protein interaction with ACE2. Since TMPRSS2 and Furin are similar across species, our data also suggest that transgenic animal models expressing human ACE2, such as the hACE2 transgenic mouse, are also likely to be useful models for studies investigating viral entry. Twit Text FOAVip Structural and functional modelling of SARS-CoV-2 entry in animal models ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=32985513 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32985513 #FOAvip English Wikipedia <ref>{{Cite pmid|32985513}}</ref> Structural and functional modelling of SARS-CoV-2 entry in animal models #MMPMID32985513 Brooke GN; Prischi F Sci Rep 2020[Sep]; 10 (1): 15917 PMID32985513show ga SARS-CoV-2 is the novel coronavirus responsible for the outbreak of COVID-19, a disease that has spread to over 100 countries and, as of the 26th July 2020, has infected over 16 million people. Despite the urgent need to find effective therapeutics, research on SARS-CoV-2 has been affected by a lack of suitable animal models. To facilitate the development of medical approaches and novel treatments, we compared the ACE2 receptor, and TMPRSS2 and Furin proteases usage of the SARS-CoV-2 Spike glycoprotein in human and in a panel of animal models, i.e. guinea pig, dog, cat, rat, rabbit, ferret, mouse, hamster and macaque. Here we showed that ACE2, but not TMPRSS2 or Furin, has a higher level of sequence variability in the Spike protein interaction surface, which greatly influences Spike protein binding mode. Using molecular docking simulations we compared the SARS-CoV and SARS-CoV-2 Spike proteins in complex with the ACE2 receptor and showed that the SARS-CoV-2 Spike glycoprotein is compatible to bind the human ACE2 with high specificity. In contrast, TMPRSS2 and Furin are sufficiently similar in the considered hosts not to drive susceptibility differences. Computational analysis of binding modes and protein contacts indicates that macaque, ferrets and hamster are the most suitable models for the study of inhibitory antibodies and small molecules targeting the SARS-CoV-2 Spike protein interaction with ACE2. Since TMPRSS2 and Furin are similar across species, our data also suggest that transgenic animal models expressing human ACE2, such as the hACE2 transgenic mouse, are also likely to be useful models for studies investigating viral entry. |Amino Acid Sequence/genetics[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Betacoronavirus/*genetics[MESH] |COVID-19[MESH] |Cats[MESH] |Computational Biology/methods[MESH] |Coronavirus Infections/pathology/*veterinary[MESH] |Cricetinae[MESH] |Disease Models, Animal[MESH] |Dogs[MESH] |Ferrets[MESH] |Furin/genetics/metabolism[MESH] |Guinea Pigs[MESH] |Humans[MESH] |Macaca fascicularis[MESH] |Mice[MESH] |Molecular Docking Simulation[MESH] |Pandemics/*veterinary[MESH] |Peptidyl-Dipeptidase A/genetics/*metabolism[MESH] |Pneumonia, Viral/pathology/*veterinary[MESH] |Rabbits[MESH] |Rats[MESH] |SARS-CoV-2[MESH] |Serine Endopeptidases/genetics/metabolism[MESH]Structural and functional modelling of SARS-CoV-2 entry in animal mode(epmc).pdf DeepDyve Pubget Overpricing