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10.1002/jmv.27339 http://scihub22266oqcxt.onion/10.1002/jmv.27339 34528721!8661603!34528721     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 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       J+Med+Virol 2022 ; 94 (1): 342-348 Nephropedia Template TP {{tp|p=34528721|t=2022. Palmitoylation of SARS-CoV-2 S protein is critical for S-mediated syncytia formation and virus entry |pdf=|usr=}}{{34528721}} gab.com Text Palmitoylation of SARS-CoV-2 S protein is critical for S-mediated syncytia formation and virus entry JO: J Med Virol http://www.kidney.de/pget.php?&tw=1&pmid=34528721 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the ongoing coronavirus disease 2019 (COVID-19) pandemic. The S protein is the key viral protein for associating with ACE2, the receptor for SARS-CoV-2. There are many kinds of posttranslational modifications in S protein. However, the detailed mechanism of palmitoylation of SARS-CoV-2 S remains to be elucidated. In our current study, we characterized the palmitoylation of SARS-CoV-2 S. Both the C15 and cytoplasmic tail of SARS-CoV-2 S were palmitoylated. Fatty acid synthase inhibitor C75 and zinc finger DHHC domain-containing palmitoyltransferase (ZDHHC) inhibitor 2-BP reduced the palmitoylation of S. Interestingly, palmitoylation of SARS-CoV-2 S was not required for plasma membrane targeting of S but was critical for S-mediated syncytia formation and SARS-CoV-2 pseudovirus particle entry. Overexpression of ZDHHC2, ZDHHC3, ZDHHC4, ZDHHC5, ZDHHC8, ZDHHC9, ZDHHC11, ZDHHC14, ZDHHC16, ZDHHC19, and ZDHHC20 promoted the palmitoylation of S. Furthermore, those ZDHHCs were identified to associate with SARS-CoV-2 S. Our study not only reveals the mechanism of S palmitoylation but also will shed important light into the role of S palmitoylation in syncytia formation and virus entry. Twit Text FOAVip Palmitoylation of SARS-CoV-2 S protein is critical for S-mediated syncytia formation and virus entry ????J Med Virol http://www.kidney.de/pget.php?&tw=1&pmid=34528721 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34528721 #FOAvip English Wikipedia <ref>{{Cite pmid|34528721}}</ref> Palmitoylation of SARS-CoV-2 S protein is critical for S-mediated syncytia formation and virus entry #MMPMID34528721 Li D; Liu Y; Lu Y; Gao S; Zhang L J Med Virol 2022[Jan]; 94 (1): 342-348 PMID34528721show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the ongoing coronavirus disease 2019 (COVID-19) pandemic. The S protein is the key viral protein for associating with ACE2, the receptor for SARS-CoV-2. There are many kinds of posttranslational modifications in S protein. However, the detailed mechanism of palmitoylation of SARS-CoV-2 S remains to be elucidated. In our current study, we characterized the palmitoylation of SARS-CoV-2 S. Both the C15 and cytoplasmic tail of SARS-CoV-2 S were palmitoylated. Fatty acid synthase inhibitor C75 and zinc finger DHHC domain-containing palmitoyltransferase (ZDHHC) inhibitor 2-BP reduced the palmitoylation of S. Interestingly, palmitoylation of SARS-CoV-2 S was not required for plasma membrane targeting of S but was critical for S-mediated syncytia formation and SARS-CoV-2 pseudovirus particle entry. Overexpression of ZDHHC2, ZDHHC3, ZDHHC4, ZDHHC5, ZDHHC8, ZDHHC9, ZDHHC11, ZDHHC14, ZDHHC16, ZDHHC19, and ZDHHC20 promoted the palmitoylation of S. Furthermore, those ZDHHCs were identified to associate with SARS-CoV-2 S. Our study not only reveals the mechanism of S palmitoylation but also will shed important light into the role of S palmitoylation in syncytia formation and virus entry. |*Virus Internalization[MESH] |4-Butyrolactone/analogs & derivatives/pharmacology[MESH] |Acyltransferases/antagonists & inhibitors[MESH] |COVID-19/pathology[MESH] |Cell Line[MESH] |Cell Membrane/*metabolism[MESH] |Giant Cells/*metabolism[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Lipoylation/*physiology[MESH] |Protein Processing, Post-Translational/physiology[MESH]Palmitoylation of SARS-CoV-2 S protein is critical for S-mediated sync(epmc).pdf DeepDyve Pubget Overpricing