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10.1016/j.virol.2017.07.019 http://scihub22266oqcxt.onion/10.1016/j.virol.2017.07.019 28738245!7111695!28738245     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28738245&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Virology 2017 ; 510 (?): 165-174 Nephropedia Template TP {{tp|p=28738245|t=2017. Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication |pdf=|usr=}}{{28738245}} gab.com Text Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication JO: Virology http://www.kidney.de/pget.php?&tw=1&pmid=28738245 #FOAvip Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection. Twit Text FOAVip Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication ????Virology http://www.kidney.de/pget.php?&tw=1&pmid=28738245 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28738245 #FOAvip English Wikipedia <ref>{{Cite pmid|28738245}}</ref> Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication #MMPMID28738245 Sakai Y; Kawachi K; Terada Y; Omori H; Matsuura Y; Kamitani W Virology 2017[Oct]; 510 (?): 165-174 PMID28738245show ga Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection. |*Amino Acid Substitution[MESH] |*Virus Replication[MESH] |DNA Mutational Analysis[MESH] |Protein Interaction Mapping[MESH] |Severe acute respiratory syndrome-related coronavirus/genetics/*physiology[MESH]Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral(epmc).pdf DeepDyve Pubget Overpricing