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10.1016/j.isci.2021.103426 http://scihub22266oqcxt.onion/10.1016/j.isci.2021.103426 34786539!8582233!34786539     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       iScience 2021 ; 24 (12): 103426 Nephropedia Template TP {{tp|p=34786539|t=2021. Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors |pdf=|usr=}}{{34786539}} gab.com Text Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors JO: iScience http://www.kidney.de/pget.php?&tw=1&pmid=34786539 #FOAvip Glycosylation of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein mediates viral entry and immune escape. While glycan site is determined by viral genetic code, glycosylation is completely dependent on host cell post-translational modification. Here, by producing SARS-CoV-2 virions from various host cell lines, viruses of different origins with diverse spike protein glycan patterns were revealed. Binding affinities to C-type lectin receptors (CLRs) DC&L-SIGN differed in the different glycan pattern virions. Although none of the CLRs supported viral productive infection, viral trans&cis-infection mediated by the CLRs were substantially changed among the different virions. Specifically, trans&cis-infection of virions with a high-mannose structure (Man(5)GlcNAc(2)) at the N1098 glycan site of the spike postfusion trimer were markedly enhanced. Considering L-SIGN co-expression with ACE2 on respiratory tract cells, our work underlines viral epigenetic glycosylation in authentic viral infection and highlights the attachment co-receptor role of DC&L-SIGN in SARS-CoV-2 infection and prevention. Twit Text FOAVip Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors ????iScience http://www.kidney.de/pget.php?&tw=1&pmid=34786539 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34786539 #FOAvip English Wikipedia <ref>{{Cite pmid|34786539}}</ref> Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors #MMPMID34786539 Guo L; Liang Y; Li H; Zheng H; Yang Z; Chen Y; Zhao X; Li J; Li B; Shi H; Sun M; Liu L iScience 2021[Dec]; 24 (12): 103426 PMID34786539show ga Glycosylation of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein mediates viral entry and immune escape. While glycan site is determined by viral genetic code, glycosylation is completely dependent on host cell post-translational modification. Here, by producing SARS-CoV-2 virions from various host cell lines, viruses of different origins with diverse spike protein glycan patterns were revealed. Binding affinities to C-type lectin receptors (CLRs) DC&L-SIGN differed in the different glycan pattern virions. Although none of the CLRs supported viral productive infection, viral trans&cis-infection mediated by the CLRs were substantially changed among the different virions. Specifically, trans&cis-infection of virions with a high-mannose structure (Man(5)GlcNAc(2)) at the N1098 glycan site of the spike postfusion trimer were markedly enhanced. Considering L-SIGN co-expression with ACE2 on respiratory tract cells, our work underlines viral epigenetic glycosylation in authentic viral infection and highlights the attachment co-receptor role of DC&L-SIGN in SARS-CoV-2 infection and prevention. äEpigenetic glycosylation of SARS-CoV-2 impact viral infection through (epmc).pdf DeepDyve Pubget Overpricing