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10.1016/j.bbamem.2021.183590 http://scihub22266oqcxt.onion/10.1016/j.bbamem.2021.183590 33621516!7896491!33621516     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33621516&cmd=llinks): Failed to open stream: HTTP request failed! 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Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance |pdf=|usr=}}{{33621516}} gab.com Text Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance JO: Biochim Biophys Acta Biomembr http://www.kidney.de/pget.php?&tw=1&pmid=33621516 #FOAvip The envelope protein E of the SARS-CoV coronavirus is an archetype of viroporin. It is a small hydrophobic protein displaying ion channel activity that has proven highly relevant in virus-host interaction and virulence. Ion transport through E channel was shown to alter Ca(2+) homeostasis in the cell and trigger inflammation processes. Here, we study transport properties of the E viroporin in mixed solutions of potassium and calcium chloride that contain a fixed total concentration (mole fraction experiments). The channel is reconstituted in planar membranes of different lipid compositions, including a lipid mixture that mimics the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane where the virus localizes within the cell. We find that the E ion conductance changes non-monotonically with the total ionic concentration displaying an Anomalous Mole Fraction Effect (AMFE) only when charged lipids are present in the membrane. We also observe that E channel insertion in ERGIC-mimic membranes - including lipid with intrinsic negative curvature - enhances ion permeation at physiological concentrations of pure CaCl(2) or KCl solutions, with a preferential transport of Ca(2+) in mixed KCl-CaCl(2) solutions. Altogether, our findings demonstrate that the presence of calcium modulates the transport properties of the E channel by interacting preferentially with charged lipids through different mechanisms including direct Coulombic interactions and possibly inducing changes in membrane morphology. Twit Text FOAVip Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance ????Biochim Biophys Acta Biomembr http://www.kidney.de/pget.php?&tw=1&pmid=33621516 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33621516 #FOAvip English Wikipedia <ref>{{Cite pmid|33621516}}</ref> Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Lipid-dependent Anomalous Mole Fraction Effect and regulation of pore conductance #MMPMID33621516 Verdia-Baguena C; Aguilella VM; Queralt-Martin M; Alcaraz A Biochim Biophys Acta Biomembr 2021[Jun]; 1863 (6): 183590 PMID33621516show ga The envelope protein E of the SARS-CoV coronavirus is an archetype of viroporin. It is a small hydrophobic protein displaying ion channel activity that has proven highly relevant in virus-host interaction and virulence. Ion transport through E channel was shown to alter Ca(2+) homeostasis in the cell and trigger inflammation processes. Here, we study transport properties of the E viroporin in mixed solutions of potassium and calcium chloride that contain a fixed total concentration (mole fraction experiments). The channel is reconstituted in planar membranes of different lipid compositions, including a lipid mixture that mimics the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane where the virus localizes within the cell. We find that the E ion conductance changes non-monotonically with the total ionic concentration displaying an Anomalous Mole Fraction Effect (AMFE) only when charged lipids are present in the membrane. We also observe that E channel insertion in ERGIC-mimic membranes - including lipid with intrinsic negative curvature - enhances ion permeation at physiological concentrations of pure CaCl(2) or KCl solutions, with a preferential transport of Ca(2+) in mixed KCl-CaCl(2) solutions. Altogether, our findings demonstrate that the presence of calcium modulates the transport properties of the E channel by interacting preferentially with charged lipids through different mechanisms including direct Coulombic interactions and possibly inducing changes in membrane morphology. |Amino Acid Sequence[MESH] |Calcium Channels/metabolism[MESH] |Calcium/*metabolism[MESH] |Ion Transport[MESH] |Membrane Lipids/metabolism[MESH] |Protein Binding[MESH] |Protein Transport[MESH] |Severe acute respiratory syndrome-related coronavirus/*metabolism[MESH] |Solutions[MESH]Transport mechanisms of SARS-CoV-E viroporin in calcium solutions: Li(epmc).pdf DeepDyve Pubget Overpricing