Tweet
Sci Rep. 2017 Dec 1;7(1):16793. doi: 10.1038/s41598-017-16986-y.
Influenza virus Matrix Protein M1 preserves its conformation with pH, changing multimerization state at the priming stage due to electrostatics.
Shtykova EV1,2, Dadinova LA1, Fedorova NV3, Golanikov AE1, Bogacheva EN2, Ksenofontov AL3, Baratova LA3, Shilova LA4,5, Tashkin VY4, Galimzyanov TR4,6, Jeffries CM7, Svergun DI7, Batishchev OV8,9.
Author information
Abstract
Influenza A virus matrix protein M1 plays an essential role in the virus lifecycle, but its functional and structural properties are not entirely defined. Here we employed small-angle X-ray scattering, atomic force microscopy and zeta-potential measurements to characterize the overall structure and association behavior of the full-length M1 at different pH conditions. We demonstrate that the protein consists of a globular N-terminal domain and a flexible C-terminal extension. The globular N-terminal domain of M1 monomers appears preserved in the range of pH from 4.0 to 6.8, while the C-terminal domain remains flexible and the tendency to form multimers changes dramatically. We found that the protein multimerization process is reversible, whereby the binding between M1 molecules starts to break around pH 6. A predicted electrostatic model of M1 self-assembly at different pH revealed a good agreement with zeta-potential measurements, allowing one to assess the role of M1 domains in M1-M1 and M1-lipid interactions. Together with the protein sequence analysis, these results provide insights into the mechanism of M1 scaffold formation and the major role of the flexible and disordered C-terminal domain in this process.
PMID: 29196731 DOI: 10.1038/s41598-017-16986-y
Free full text
Influenza virus Matrix Protein M1 preserves its conformation with pH, changing multimerization state at the priming stage due to electrostatics.
Shtykova EV1,2, Dadinova LA1, Fedorova NV3, Golanikov AE1, Bogacheva EN2, Ksenofontov AL3, Baratova LA3, Shilova LA4,5, Tashkin VY4, Galimzyanov TR4,6, Jeffries CM7, Svergun DI7, Batishchev OV8,9.
Author information
Abstract
Influenza A virus matrix protein M1 plays an essential role in the virus lifecycle, but its functional and structural properties are not entirely defined. Here we employed small-angle X-ray scattering, atomic force microscopy and zeta-potential measurements to characterize the overall structure and association behavior of the full-length M1 at different pH conditions. We demonstrate that the protein consists of a globular N-terminal domain and a flexible C-terminal extension. The globular N-terminal domain of M1 monomers appears preserved in the range of pH from 4.0 to 6.8, while the C-terminal domain remains flexible and the tendency to form multimers changes dramatically. We found that the protein multimerization process is reversible, whereby the binding between M1 molecules starts to break around pH 6. A predicted electrostatic model of M1 self-assembly at different pH revealed a good agreement with zeta-potential measurements, allowing one to assess the role of M1 domains in M1-M1 and M1-lipid interactions. Together with the protein sequence analysis, these results provide insights into the mechanism of M1 scaffold formation and the major role of the flexible and disordered C-terminal domain in this process.
PMID: 29196731 DOI: 10.1038/s41598-017-16986-y
Free full text