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10.1038/s41598-021-04133-7 http://scihub22266oqcxt.onion/10.1038/s41598-021-04133-7 34952919!8709866!34952919     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       Sci+Rep 2021 ; 11 (1): 24432 Nephropedia Template TP {{tp|p=34952919|t=2021. Modulation of the NLRP3 inflammasome by Sars-CoV-2 Envelope protein |pdf=|usr=}}{{34952919}} gab.com Text Modulation of the NLRP3 inflammasome by Sars-CoV-2 Envelope protein JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=34952919 #FOAvip Despite the initial success of some drugs and vaccines targeting COVID-19, understanding the mechanism underlying SARS-CoV-2 disease pathogenesis remains crucial for the development of further approaches to treatment. Some patients with severe Covid-19 experience a cytokine storm and display evidence of inflammasome activation leading to increased levels of IL-1beta and IL-18; however, other reports have suggested reduced inflammatory responses to Sars-Cov-2. In this study we have examined the effects of the Sars-Cov-2 envelope (E) protein, a virulence factor in coronaviruses, on inflammasome activation and pulmonary inflammation. In cultured macrophages the E protein suppressed inflammasome priming and NLRP3 inflammasome activation. Similarly, in mice transfected with E protein and treated with poly(I:C) to simulate the effects of viral RNA, the E protein, in an NLRP3-dependent fashion, reduced expression of pro-IL-1beta, levels of IL-1beta and IL-18 in broncho-alveolar lavage fluid, and macrophage infiltration in the lung. To simulate the effects of more advanced infection, macrophages were treated with both LPS and poly(I:C). In this setting the E protein increased NLRP3 inflammasome activation in both murine and human macrophages. Thus, the Sars-Cov-2 E protein may initially suppress the host NLRP3 inflammasome response to viral RNA while potentially increasing NLRP3 inflammasome responses in the later stages of infection. Targeting the Sars-Cov-2 E protein especially in the early stages of infection may represent a novel approach to Covid-19 therapy. Twit Text FOAVip Modulation of the NLRP3 inflammasome by Sars-CoV-2 Envelope protein ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=34952919 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34952919 #FOAvip English Wikipedia <ref>{{Cite pmid|34952919}}</ref> Modulation of the NLRP3 inflammasome by Sars-CoV-2 Envelope protein #MMPMID34952919 Yalcinkaya M; Liu W; Islam MN; Kotini AG; Gusarova GA; Fidler TP; Papapetrou EP; Bhattacharya J; Wang N; Tall AR Sci Rep 2021[Dec]; 11 (1): 24432 PMID34952919show ga Despite the initial success of some drugs and vaccines targeting COVID-19, understanding the mechanism underlying SARS-CoV-2 disease pathogenesis remains crucial for the development of further approaches to treatment. Some patients with severe Covid-19 experience a cytokine storm and display evidence of inflammasome activation leading to increased levels of IL-1beta and IL-18; however, other reports have suggested reduced inflammatory responses to Sars-Cov-2. In this study we have examined the effects of the Sars-Cov-2 envelope (E) protein, a virulence factor in coronaviruses, on inflammasome activation and pulmonary inflammation. In cultured macrophages the E protein suppressed inflammasome priming and NLRP3 inflammasome activation. Similarly, in mice transfected with E protein and treated with poly(I:C) to simulate the effects of viral RNA, the E protein, in an NLRP3-dependent fashion, reduced expression of pro-IL-1beta, levels of IL-1beta and IL-18 in broncho-alveolar lavage fluid, and macrophage infiltration in the lung. To simulate the effects of more advanced infection, macrophages were treated with both LPS and poly(I:C). In this setting the E protein increased NLRP3 inflammasome activation in both murine and human macrophages. Thus, the Sars-Cov-2 E protein may initially suppress the host NLRP3 inflammasome response to viral RNA while potentially increasing NLRP3 inflammasome responses in the later stages of infection. Targeting the Sars-Cov-2 E protein especially in the early stages of infection may represent a novel approach to Covid-19 therapy. |Animals[MESH] |Bronchoalveolar Lavage Fluid/chemistry[MESH] |COVID-19/pathology/virology[MESH] |Coronavirus Envelope Proteins/genetics/*metabolism[MESH] |Down-Regulation/drug effects[MESH] |Endoplasmic Reticulum Stress[MESH] |Humans[MESH] |Inflammasomes/drug effects/*metabolism[MESH] |Interleukin-1beta/genetics/metabolism[MESH] |Janus Kinases/genetics/metabolism[MESH] |Lipopolysaccharides/pharmacology[MESH] |Macrophages/cytology/drug effects/metabolism[MESH] |Mice[MESH] |Mice, Inbred C57BL[MESH] |Mice, Knockout[MESH] |NLR Family, Pyrin Domain-Containing 3 Protein/deficiency/genetics/*metabolism[MESH] |Poly I-C/pharmacology[MESH] |RNA, Viral/metabolism[MESH]Modulation of the NLRP3 inflammasome by Sars-CoV-2 Envelope protein (epmc).pdf DeepDyve Pubget Overpricing