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10.3389/fmolb.2021.607443 http://scihub22266oqcxt.onion/10.3389/fmolb.2021.607443 33659275!7917183!33659275     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Mol+Biosci 2021 ; 8 (ä): 607443 Nephropedia Template TP {{tp|p=33659275|t=2021. Molecular Mechanisms Behind Anti SARS-CoV-2 Action of Lactoferrin |pdf=|usr=}}{{33659275}} gab.com Text Molecular Mechanisms Behind Anti SARS-CoV-2 Action of Lactoferrin JO: Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=33659275 #FOAvip Despite the huge effort to contain the infection, the novel SARS-CoV-2 coronavirus has rapidly become pandemic, mainly due to its extremely high human-to-human transmission capability, and a surprisingly high viral charge of symptom-less people. While the seek for a vaccine is still ongoing, promising results have been obtained with antiviral compounds. In particular, lactoferrin is regarded to have beneficial effects both in preventing and soothing the infection. Here, we explore the possible molecular mechanisms with which lactoferrin interferes with SARS-CoV-2 cell invasion, preventing attachment and/or entry of the virus. To this aim, we search for possible interactions lactoferrin may have with virus structural proteins and host receptors. Representing the molecular iso-electron surface of proteins in terms of 2D-Zernike descriptors, we 1) identified putative regions on the lactoferrin surface able to bind sialic acid present on the host cell membrane, sheltering the cell from the virus attachment; 2) showed that no significant shape complementarity is present between lactoferrin and the ACE2 receptor, while 3) two high complementarity regions are found on the N- and C-terminal domains of the SARS-CoV-2 spike protein, hinting at a possible competition between lactoferrin and ACE2 for the binding to the spike protein. Twit Text FOAVip Molecular Mechanisms Behind Anti SARS-CoV-2 Action of Lactoferrin ????Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=33659275 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33659275 #FOAvip English Wikipedia <ref>{{Cite pmid|33659275}}</ref> Molecular Mechanisms Behind Anti SARS-CoV-2 Action of Lactoferrin #MMPMID33659275 Miotto M; Di Rienzo L; Bo L; Boffi A; Ruocco G; Milanetti E Front Mol Biosci 2021[]; 8 (ä): 607443 PMID33659275show ga Despite the huge effort to contain the infection, the novel SARS-CoV-2 coronavirus has rapidly become pandemic, mainly due to its extremely high human-to-human transmission capability, and a surprisingly high viral charge of symptom-less people. While the seek for a vaccine is still ongoing, promising results have been obtained with antiviral compounds. In particular, lactoferrin is regarded to have beneficial effects both in preventing and soothing the infection. Here, we explore the possible molecular mechanisms with which lactoferrin interferes with SARS-CoV-2 cell invasion, preventing attachment and/or entry of the virus. To this aim, we search for possible interactions lactoferrin may have with virus structural proteins and host receptors. Representing the molecular iso-electron surface of proteins in terms of 2D-Zernike descriptors, we 1) identified putative regions on the lactoferrin surface able to bind sialic acid present on the host cell membrane, sheltering the cell from the virus attachment; 2) showed that no significant shape complementarity is present between lactoferrin and the ACE2 receptor, while 3) two high complementarity regions are found on the N- and C-terminal domains of the SARS-CoV-2 spike protein, hinting at a possible competition between lactoferrin and ACE2 for the binding to the spike protein. äMolecular Mechanisms Behind Anti SARS-CoV-2 Action of Lactoferrin (epmc).pdf DeepDyve Pubget Overpricing