tetano
Editor, Senior Moderator
Biosci Rep. 2019 Jul 19. pii: BSR20191024. doi: 10.1042/BSR20191024. [Epub ahead of print]
[h=1]Influenza A matrix protein M1 induces lipid membrane deformation via protein multimerization.[/h] Dahmani I[SUP]1[/SUP], Ludwig K[SUP]2[/SUP], Chiantia S[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The matrix protein M1 of the Influenza A virus is supposed to mediate viral assembly and budding at the plasma membrane (PM) of infected cells. In order for a new viral particle to form, the PM lipid bilayer has to bend into a vesicle towards the extracellular side. Studies in cellular models have proposed that different viral proteins might be responsible for inducing membrane curvature in this context (including M1), but a clear consensus has not been reached. In this study, we use a combination of fluorescence microscopy, cryogenic transmission electron microscopy (cryo-TEM), cryo-electron tomography (cryo-ET) and scanning fluorescence correlation spectroscopy (sFCS) to investigate M1-induced membrane deformation in biophysical models of the PM. Our results indicate that M1 is indeed able to cause membrane curvature in lipid bilayers containing negatively-charged lipids, in the absence of other viral components. Furthermore, we prove that protein binding is not sufficient to induce membrane restructuring. Rather, it appears that stable M1-M1 interactions and multimer formation are required in order to alter the bilayer three-dimensional structure, through the formation of a protein scaffold. Finally, our results suggest that, in a physiological context, M1-induced membrane deformation might be modulated by the initial bilayer curvature and the lateral organization of membrane components (i.e. the presence of lipid domains).
?2019 The Author(s).
[h=4]KEYWORDS:[/h] confocal microscopy; influenza; lipid membranes; membranes; protein-protein interactions; viral matrix proteins
PMID: 31324731 DOI: 10.1042/BSR20191024
[h=1]Influenza A matrix protein M1 induces lipid membrane deformation via protein multimerization.[/h] Dahmani I[SUP]1[/SUP], Ludwig K[SUP]2[/SUP], Chiantia S[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The matrix protein M1 of the Influenza A virus is supposed to mediate viral assembly and budding at the plasma membrane (PM) of infected cells. In order for a new viral particle to form, the PM lipid bilayer has to bend into a vesicle towards the extracellular side. Studies in cellular models have proposed that different viral proteins might be responsible for inducing membrane curvature in this context (including M1), but a clear consensus has not been reached. In this study, we use a combination of fluorescence microscopy, cryogenic transmission electron microscopy (cryo-TEM), cryo-electron tomography (cryo-ET) and scanning fluorescence correlation spectroscopy (sFCS) to investigate M1-induced membrane deformation in biophysical models of the PM. Our results indicate that M1 is indeed able to cause membrane curvature in lipid bilayers containing negatively-charged lipids, in the absence of other viral components. Furthermore, we prove that protein binding is not sufficient to induce membrane restructuring. Rather, it appears that stable M1-M1 interactions and multimer formation are required in order to alter the bilayer three-dimensional structure, through the formation of a protein scaffold. Finally, our results suggest that, in a physiological context, M1-induced membrane deformation might be modulated by the initial bilayer curvature and the lateral organization of membrane components (i.e. the presence of lipid domains).
?2019 The Author(s).
[h=4]KEYWORDS:[/h] confocal microscopy; influenza; lipid membranes; membranes; protein-protein interactions; viral matrix proteins
PMID: 31324731 DOI: 10.1042/BSR20191024