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10.1021/acscentsci.0c01537 http://scihub22266oqcxt.onion/10.1021/acscentsci.0c01537 34341769!8265543!34341769     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       ACS+Cent+Sci 2021 ; 7 (7): 1156-1165 Nephropedia Template TP {{tp|p=34341769|t=2021. CD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV-2 |pdf=|usr=}}{{34341769}} gab.com Text CD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV-2 JO: ACS Cent Sci http://www.kidney.de/pget.php?&tw=1&pmid=34341769 #FOAvip As the COVID-19 pandemic continues to spread, investigating the processes underlying the interactions between SARS-CoV-2 and its hosts is of high importance. Here, we report the identification of CD209L/L-SIGN and the related protein CD209/DC-SIGN as receptors capable of mediating SARS-CoV-2 entry into human cells. Immunofluorescence staining of human tissues revealed prominent expression of CD209L in the lung and kidney epithelia and endothelia. Multiple biochemical assays using a purified recombinant SARS-CoV-2 spike receptor-binding domain (S-RBD) or S1 encompassing both N termal domain and RBD and ectopically expressed CD209L and CD209 revealed that CD209L and CD209 interact with S-RBD. CD209L contains two N-glycosylation sequons, at sites N92 and N361, but we determined that only site N92 is occupied. Removal of the N-glycosylation at this site enhances the binding of S-RBD with CD209L. CD209L also interacts with ACE2, suggesting a role for heterodimerization of CD209L and ACE2 in SARS-CoV-2 entry and infection in cell types where both are present. Furthermore, we demonstrate that human endothelial cells are permissive to SARS-CoV-2 infection, and interference with CD209L activity by a knockdown strategy or with soluble CD209L inhibits virus entry. Our observations demonstrate that CD209L and CD209 serve as alternative receptors for SARS-CoV-2 in disease-relevant cell types, including the vascular system. This property is particularly important in tissues where ACE2 has low expression or is absent and may have implications for antiviral drug development. Twit Text FOAVip CD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV-2 ????ACS Cent Sci http://www.kidney.de/pget.php?&tw=1&pmid=34341769 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34341769 #FOAvip English Wikipedia <ref>{{Cite pmid|34341769}}</ref> CD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV-2 #MMPMID34341769 Amraei R; Yin W; Napoleon MA; Suder EL; Berrigan J; Zhao Q; Olejnik J; Chandler KB; Xia C; Feldman J; Hauser BM; Caradonna TM; Schmidt AG; Gummuluru S; Muhlberger E; Chitalia V; Costello CE; Rahimi N ACS Cent Sci 2021[Jul]; 7 (7): 1156-1165 PMID34341769show ga As the COVID-19 pandemic continues to spread, investigating the processes underlying the interactions between SARS-CoV-2 and its hosts is of high importance. Here, we report the identification of CD209L/L-SIGN and the related protein CD209/DC-SIGN as receptors capable of mediating SARS-CoV-2 entry into human cells. Immunofluorescence staining of human tissues revealed prominent expression of CD209L in the lung and kidney epithelia and endothelia. Multiple biochemical assays using a purified recombinant SARS-CoV-2 spike receptor-binding domain (S-RBD) or S1 encompassing both N termal domain and RBD and ectopically expressed CD209L and CD209 revealed that CD209L and CD209 interact with S-RBD. CD209L contains two N-glycosylation sequons, at sites N92 and N361, but we determined that only site N92 is occupied. Removal of the N-glycosylation at this site enhances the binding of S-RBD with CD209L. CD209L also interacts with ACE2, suggesting a role for heterodimerization of CD209L and ACE2 in SARS-CoV-2 entry and infection in cell types where both are present. Furthermore, we demonstrate that human endothelial cells are permissive to SARS-CoV-2 infection, and interference with CD209L activity by a knockdown strategy or with soluble CD209L inhibits virus entry. Our observations demonstrate that CD209L and CD209 serve as alternative receptors for SARS-CoV-2 in disease-relevant cell types, including the vascular system. This property is particularly important in tissues where ACE2 has low expression or is absent and may have implications for antiviral drug development. äCD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV-2 (epmc).pdf DeepDyve Pubget Overpricing