tetano
Editor, Senior Moderator
Biophys J
. 2021 Nov 19;S0006-3495(21)00992-9.
doi: 10.1016/j.bpj.2021.11.023. Online ahead of print.
Influenza A M2 recruits M1 to the plasma membrane: a fluorescence fluctuation microscopy study
Annett Petrich[SUP] 1 [/SUP], Valentin Dunsing[SUP] 1 [/SUP], Sara Bobone[SUP] 2 [/SUP], Salvatore Chiantia[SUP] 3 [/SUP]
Affiliations
Abstract
Influenza A virus (IAV) is a respiratory pathogen that causes seasonal epidemics with significant mortality. One of the most abundant proteins in IAV particles is the matrix protein 1 (M1), which is essential for the virus structural stability. M1 organizes virion assembly and budding at the plasma membrane (PM), where it interacts with other viral components. The recruitment of M1 to the PM as well as its interaction with the other viral envelope proteins (hemagglutinin (HA), neuraminidase, matrix protein 2 (M2)) is controversially discussed in previous studies. Therefore, we used fluorescence fluctuation microscopy techniques (i.e., scanning fluorescence cross-correlation spectroscopy and Number and Brightness) to quantify the oligomeric state of M1 and its interactions with other viral proteins in co-transfected as well as infected cells. Our results indicate that M1 is recruited to the PM by M2, as a consequence of the strong interaction between the two proteins. In contrast, only a weak interaction between M1 and HA was observed. M1-HA interaction occurred only in the case that M1 was already bound to the PM. We therefore conclude that M2 initiates the assembly of IAV by recruiting M1 to the PM, possibly allowing its further interaction with other viral proteins.
Keywords: Number and Brightness; fluorescence correlation spectroscopy; fluorescence fluctuation spectroscopy; fluorescence microscopy; hemagglutinin; influenza; matrix protein 1; matrix protein 2; neuraminidase; plasma membrane; protein-protein interaction; virus assembly.
. 2021 Nov 19;S0006-3495(21)00992-9.
doi: 10.1016/j.bpj.2021.11.023. Online ahead of print.
Influenza A M2 recruits M1 to the plasma membrane: a fluorescence fluctuation microscopy study
Annett Petrich[SUP] 1 [/SUP], Valentin Dunsing[SUP] 1 [/SUP], Sara Bobone[SUP] 2 [/SUP], Salvatore Chiantia[SUP] 3 [/SUP]
Affiliations
- PMID: 34808098
- DOI: 10.1016/j.bpj.2021.11.023
Abstract
Influenza A virus (IAV) is a respiratory pathogen that causes seasonal epidemics with significant mortality. One of the most abundant proteins in IAV particles is the matrix protein 1 (M1), which is essential for the virus structural stability. M1 organizes virion assembly and budding at the plasma membrane (PM), where it interacts with other viral components. The recruitment of M1 to the PM as well as its interaction with the other viral envelope proteins (hemagglutinin (HA), neuraminidase, matrix protein 2 (M2)) is controversially discussed in previous studies. Therefore, we used fluorescence fluctuation microscopy techniques (i.e., scanning fluorescence cross-correlation spectroscopy and Number and Brightness) to quantify the oligomeric state of M1 and its interactions with other viral proteins in co-transfected as well as infected cells. Our results indicate that M1 is recruited to the PM by M2, as a consequence of the strong interaction between the two proteins. In contrast, only a weak interaction between M1 and HA was observed. M1-HA interaction occurred only in the case that M1 was already bound to the PM. We therefore conclude that M2 initiates the assembly of IAV by recruiting M1 to the PM, possibly allowing its further interaction with other viral proteins.
Keywords: Number and Brightness; fluorescence correlation spectroscopy; fluorescence fluctuation spectroscopy; fluorescence microscopy; hemagglutinin; influenza; matrix protein 1; matrix protein 2; neuraminidase; plasma membrane; protein-protein interaction; virus assembly.