Study of adsorption of Influenza virus matrix protein M1 on lipid membranes by the technique of fluorescent probes

被引：6

作者：

Shilova L.A. ^{[1
,2
]}

Knyazev D.G. ^{[3
]}

Fedorova N.V. ^{[4
]}

Shtykova E.V. ^{[5
]}

Batishchev O.V. ^{[1
]}

机构：

[1] Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, Leninskii pr. 31, build. 4, Moscow

[2] Moscow Institute of Physics and Technology (State University), Institutskii per. 9, Dolgoprudny, Moscow oblast

[3] Institute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, Linz

[4] Belozersky Institute of Physico-Chemical Biology, Moscow Lomonosov State University, Leninskie Gory 1, build. 40, Moscow

[5] Federal Scientific and Research Center Crystallography and Fotonics, Russian Academy of Sciences, Leninskii pr. 59, Moscow

来源：

Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology | 2017年 / 11卷 / 3期

基金：

俄罗斯科学基金会;

关键词：

adsorption; fluorescent probes; Influenza A virus; matrix protein M1; protein–lipid interactions;

D O I：

10.1134/S1990747817030072

中图分类号：

学科分类号：

摘要：

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. © 2017, Pleiades Publishing, Ltd.

引用

页码：225 / 230

页数：5

共 30 条

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