tetano
Editor, Senior Moderator
FEBS Lett. 2018 Jun 22. doi: 10.1002/1873-3468.13172. [Epub ahead of print]
[h=1]Composition-dependent Membrane Disruption by the Proapoptotic Protein PB1F2 from HK97 Influenza A Virus.[/h] Wang Y[SUP]1,[/SUP][SUP]2[/SUP], Yang J[SUP]1,[/SUP][SUP]2[/SUP], Wang J[SUP]1,[/SUP][SUP]2[/SUP], Zhu L[SUP]1,[/SUP][SUP]2[/SUP], Wang J[SUP]1,[/SUP][SUP]2,[/SUP][SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] PB1F2 is a proapoptotic protein encoded by an alternative reading frame in the influenza A virus. Its accumulation accelerates mitochondrial fragmentation by decreasing the mitochondrial membrane potential following translocation into the mitochondrial inner membrane space, but the mechanistic underpinnings remain unclear. Herein, the PB1F2 from HK97 was expressed and purified in soluble form. The interaction between PB1F2 and the mitochondrial membrane were investigated using three membrane mimics, liposomes, bicelles and nanodiscs. We show that the interactions between PB1F2 and membrane mimics depend on lipid type and are time- and dose-dependent. The primary membrane target of PB1F2 is phosphatidylcholine, the lipid that forms the major component of mitochondrial inner membranes. PB1F2 disrupts the integrity of lipid membranes by forming micelle-like PB1F2-lipid assemblies. This article is protected by copyright. All rights reserved.
[h=4]KEYWORDS:[/h] NMR ; Influenza A virus; PB1F2; membrane disruption; micelle-like lipid assembly
PMID: 29933499 DOI: 10.1002/1873-3468.13172
[h=1]Composition-dependent Membrane Disruption by the Proapoptotic Protein PB1F2 from HK97 Influenza A Virus.[/h] Wang Y[SUP]1,[/SUP][SUP]2[/SUP], Yang J[SUP]1,[/SUP][SUP]2[/SUP], Wang J[SUP]1,[/SUP][SUP]2[/SUP], Zhu L[SUP]1,[/SUP][SUP]2[/SUP], Wang J[SUP]1,[/SUP][SUP]2,[/SUP][SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] PB1F2 is a proapoptotic protein encoded by an alternative reading frame in the influenza A virus. Its accumulation accelerates mitochondrial fragmentation by decreasing the mitochondrial membrane potential following translocation into the mitochondrial inner membrane space, but the mechanistic underpinnings remain unclear. Herein, the PB1F2 from HK97 was expressed and purified in soluble form. The interaction between PB1F2 and the mitochondrial membrane were investigated using three membrane mimics, liposomes, bicelles and nanodiscs. We show that the interactions between PB1F2 and membrane mimics depend on lipid type and are time- and dose-dependent. The primary membrane target of PB1F2 is phosphatidylcholine, the lipid that forms the major component of mitochondrial inner membranes. PB1F2 disrupts the integrity of lipid membranes by forming micelle-like PB1F2-lipid assemblies. This article is protected by copyright. All rights reserved.
[h=4]KEYWORDS:[/h] NMR ; Influenza A virus; PB1F2; membrane disruption; micelle-like lipid assembly
PMID: 29933499 DOI: 10.1002/1873-3468.13172