Study of adsorption of Influenza virus matrix protein M1 on lipid membranes by the technique of fluorescent probes
- Authors: Shilova L.A.1,2, Knyazev D.G.3, Fedorova N.V.4, Shtykova E.V.5, Batishchev O.V.1
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Affiliations:
- Frumkin Institute of Physical Chemistry and Electrochemistry
- Moscow Institute of Physics and Technology (State University)
- Institute of Biophysics
- Belozersky Institute of Physico-Chemical Biology
- Federal Scientific and Research Center Crystallography and Fotonics
- Issue: Vol 11, No 3 (2017)
- Pages: 225-230
- Section: Articles
- URL: https://journals.rcsi.science/1990-7478/article/view/213256
- DOI: https://doi.org/10.1134/S1990747817030072
- ID: 213256
Cite item
Abstract
Matrix protein M1 of Influenza virus, which forms its inner scaffold, is the most abundant amongst viral proteins. Functions of M1 protein are highly diverse, as it has to ensure both the entry of the viral genetic material into the cytoplasm of the infected cell and the assembly of new viral particles for multiplication of infection. In all these processes matrix protein interacts with lipid membranes–either viral external lipid envelope or plasma membrane of a virus-infected cell. However, molecular mechanisms of such interactions are still unclear. In this work, we used the method of fluorescent probes on the example of 1-anilinonaphthalene- 8-sulfonate to determine components of the lipid bilayer required for binding of the M1 protein to the membrane, as well as possible orientations of the protein relative to the lipid membrane. We found that for the adsorption of matrix protein M1 lipid bilayer had to contain phosphatidylserines, while neither phosphatidylethanolamine nor cholesterol promoted protein binding to the membrane. Furthermore, our data suggest that M1 protein binds negatively charged lipid bilayer by positively charged amino acids exhibiting outward anionic sites.
About the authors
L. A. Shilova
Frumkin Institute of Physical Chemistry and Electrochemistry; Moscow Institute of Physics and Technology (State University)
Email: olegbati@gmail.com
Russian Federation, Leninskii pr. 31, build. 4, Moscow, 119071; Institutskii per. 9, Dolgoprudny, Moscow oblast, 141700
D. G. Knyazev
Institute of Biophysics
Email: olegbati@gmail.com
Austria, Gruberstrasse 40, Linz, A-4020
N. V. Fedorova
Belozersky Institute of Physico-Chemical Biology
Email: olegbati@gmail.com
Russian Federation, Leninskie Gory 1, build. 40, Moscow, 119991
E. V. Shtykova
Federal Scientific and Research Center Crystallography and Fotonics
Email: olegbati@gmail.com
Russian Federation, Leninskii pr. 59, Moscow, 119333
O. V. Batishchev
Frumkin Institute of Physical Chemistry and Electrochemistry
Author for correspondence.
Email: olegbati@gmail.com
Russian Federation, Leninskii pr. 31, build. 4, Moscow, 119071