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10.7554/eLife.58537 http://scihub22266oqcxt.onion/10.7554/eLife.58537 33112230!7665892!33112230     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Elife 2020 ; 9 (ä): ä Nephropedia Template TP {{tp|p=33112230|t=2020. Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state |pdf=|usr=}}{{33112230}} gab.com Text Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state JO: Elife http://www.kidney.de/pget.php?&tw=1&pmid=33112230 #FOAvip The interferon-inducible transmembrane (IFITM) proteins belong to the Dispanin/CD225 family and inhibit diverse virus infections. IFITM3 reduces membrane fusion between cells and virions through a poorly characterized mechanism. Mutation of proline-rich transmembrane protein 2 (PRRT2), a regulator of neurotransmitter release, at glycine-305 was previously linked to paroxysmal neurological disorders in humans. Here, we show that glycine-305 and the homologous site in IFITM3, glycine-95, drive protein oligomerization from within a GxxxG motif. Mutation of glycine-95 (and to a lesser extent, glycine-91) disrupted IFITM3 oligomerization and reduced its antiviral activity against Influenza A virus. An oligomerization-defective variant was used to reveal that IFITM3 promotes membrane rigidity in a glycine-95-dependent and amphipathic helix-dependent manner. Furthermore, a compound which counteracts virus inhibition by IFITM3, Amphotericin B, prevented the IFITM3-mediated rigidification of membranes. Overall, these data suggest that IFITM3 oligomers inhibit virus-cell fusion by promoting membrane rigidity. Twit Text FOAVip Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state ????Elife http://www.kidney.de/pget.php?&tw=1&pmid=33112230 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33112230 #FOAvip English Wikipedia <ref>{{Cite pmid|33112230}}</ref> Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state #MMPMID33112230 Rahman K; Coomer CA; Majdoul S; Ding SY; Padilla-Parra S; Compton AA Elife 2020[Oct]; 9 (ä): ä PMID33112230show ga The interferon-inducible transmembrane (IFITM) proteins belong to the Dispanin/CD225 family and inhibit diverse virus infections. IFITM3 reduces membrane fusion between cells and virions through a poorly characterized mechanism. Mutation of proline-rich transmembrane protein 2 (PRRT2), a regulator of neurotransmitter release, at glycine-305 was previously linked to paroxysmal neurological disorders in humans. Here, we show that glycine-305 and the homologous site in IFITM3, glycine-95, drive protein oligomerization from within a GxxxG motif. Mutation of glycine-95 (and to a lesser extent, glycine-91) disrupted IFITM3 oligomerization and reduced its antiviral activity against Influenza A virus. An oligomerization-defective variant was used to reveal that IFITM3 promotes membrane rigidity in a glycine-95-dependent and amphipathic helix-dependent manner. Furthermore, a compound which counteracts virus inhibition by IFITM3, Amphotericin B, prevented the IFITM3-mediated rigidification of membranes. Overall, these data suggest that IFITM3 oligomers inhibit virus-cell fusion by promoting membrane rigidity. |Amino Acid Motifs[MESH] |Cell Line[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Influenza A virus/genetics/*physiology[MESH] |Influenza, Human/genetics/*immunology/virology[MESH] |Membrane Proteins/*chemistry/genetics/*immunology[MESH] |RNA-Binding Proteins/*chemistry/genetics/*immunology[MESH]Homology-guided identification of a conserved motif linking the antivi(epmc).pdf DeepDyve Pubget Overpricing