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10.1093/jb/mvac054 http://scihub22266oqcxt.onion/10.1093/jb/mvac054 35792074!9278198!35792074     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\35792074.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biochem 2022 ; 172 (4): 205-216 Nephropedia Template TP {{tp|p=35792074|t=2022. Cloaking the ACE2 receptor with salivary cationic proteins inhibits SARS-CoV-2 entry |pdf=|usr=}}{{35792074}} gab.com Text Cloaking the ACE2 receptor with salivary cationic proteins inhibits SARS-CoV-2 entry JO: J Biochem http://www.kidney.de/pget.php?&tw=1&pmid=35792074 #FOAvip Saliva contributes to the innate immune system, which suggests that it can prevent SARS-CoV-2 entry. We studied the ability of healthy salivary proteins to bind to angiotensin-converting enzyme 2 (ACE2) using biolayer interferometry and pull-down assays. Their effects on binding between the receptor-binding domain of the SARS-CoV-2 spike protein S1 (S1) and ACE2 were determined using an enzyme-linked immunosorbent assay. Saliva bound to ACE2 and disrupted the binding of S1 to ACE2 and four ACE2-binding salivary proteins were identified, including cationic histone H2A and neutrophil elastase, which inhibited the S1-ACE2 interaction. Calf thymus histone (ct-histone) also inhibited binding as effectively as histone H2A. The results of a cell-based infection assay indicated that ct-histone suppressed SARS-CoV-2 pseudoviral invasion into ACE2-expressing host cells. Manufactured polypeptides, such as epsilon-poly-L-lysine, also disrupted S1-ACE2 binding, indicating the importance of the cationic properties of salivary proteins in ACE2 binding. Overall, we demonstrated that positively charged salivary proteins are a barrier against SARS-CoV-2 entry by cloaking the negatively charged surface of ACE2 and provided a view that the cationic polypeptides represent a preventative and therapeutic treatment against COVID-19. Twit Text FOAVip Cloaking the ACE2 receptor with salivary cationic proteins inhibits SARS-CoV-2 entry ????J Biochem http://www.kidney.de/pget.php?&tw=1&pmid=35792074 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35792074 #FOAvip English Wikipedia <ref>{{Cite pmid|35792074}}</ref> Cloaking the ACE2 receptor with salivary cationic proteins inhibits SARS-CoV-2 entry #MMPMID35792074 Yoshizato K; Taira T; Sato-Matsubara M; Sekiguchi S; Yabunaka Y; Kira Y; Ohashi T; Daikoku A; Ofusa K; Kadono C; Oikawa D; Matsubara T; Nakagama Y; Kido Y; Tokunaga F; Ikeda K; Kaneko A; Kawada N J Biochem 2022[Sep]; 172 (4): 205-216 PMID35792074show ga Saliva contributes to the innate immune system, which suggests that it can prevent SARS-CoV-2 entry. We studied the ability of healthy salivary proteins to bind to angiotensin-converting enzyme 2 (ACE2) using biolayer interferometry and pull-down assays. Their effects on binding between the receptor-binding domain of the SARS-CoV-2 spike protein S1 (S1) and ACE2 were determined using an enzyme-linked immunosorbent assay. Saliva bound to ACE2 and disrupted the binding of S1 to ACE2 and four ACE2-binding salivary proteins were identified, including cationic histone H2A and neutrophil elastase, which inhibited the S1-ACE2 interaction. Calf thymus histone (ct-histone) also inhibited binding as effectively as histone H2A. The results of a cell-based infection assay indicated that ct-histone suppressed SARS-CoV-2 pseudoviral invasion into ACE2-expressing host cells. Manufactured polypeptides, such as epsilon-poly-L-lysine, also disrupted S1-ACE2 binding, indicating the importance of the cationic properties of salivary proteins in ACE2 binding. Overall, we demonstrated that positively charged salivary proteins are a barrier against SARS-CoV-2 entry by cloaking the negatively charged surface of ACE2 and provided a view that the cationic polypeptides represent a preventative and therapeutic treatment against COVID-19. |*Angiotensin-Converting Enzyme 2[MESH] |*COVID-19[MESH] |Histones/metabolism[MESH] |Humans[MESH] |Leukocyte Elastase/metabolism[MESH] |Peptidyl-Dipeptidase A/metabolism[MESH] |Polylysine/metabolism[MESH] |Protein Binding[MESH] |SARS-CoV-2[MESH] |Salivary Proteins and Peptides/metabolism/pharmacology[MESH]Cloaking the ACE2 receptor with salivary cationic proteins inhibits SA(epmc).pdf DeepDyve Pubget Overpricing