Modeling of the Interaction of Viral Fusion Peptides with the Domains of Liquid-Ordered Phase in a Lipid Membrane
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Membrane microdomains enriched with sphingomyelin and cholesterol, the so-called rafts, are thicker than the surrounding membrane. To smooth the thickness mismatch, the membrane is deformed, which leads to the formation of a complex asymmetric structure of the raft boundary. The rafts are of great importance in the process of viral infection of the cell: for example, in recent experiments it has been shown that the fusion peptide of human immunodeficiency virus (HIV) tends to be predominantly inserted at the raft boundary, and the effectiveness of the fusion was low in the absence of the rafts. It has been noticed in these studies that such preferential distribution of fusion peptides was not found in the case of influenza virus. In the present paper, we modeled the interaction of fusion peptides with rafts by the methods of elasticity theory of lipid membranes. We have shown that the boundary of the liquid-ordered domains can act as an attractor for the fusion peptides: peptides distribute to the raft boundary and play the role of line-active membrane components. Our model enables to explain the difference of the behavior of different fusion peptides in the presence of rafts in the above mentioned example of the experimental data by different geometry of their insertion into the lipid monolayer. Our results show the fundamental mechanisms by which the geometry of fusion peptide insertion affects their distribution in the lipid membrane.
Keywords:lipid membranes theory of elasticity of lipid membranes rafts fusion peptides
ACKNOWLEDGMENTS COMPLIANCE WITH ETHICAL STANDARDS
The work was supported by the grant of the President of the Russian Federation (project no. MK-1807.2017.4) and by the Russian Foundation for Basic Research (project nos. 17-54-30022 and 17-04-02070).
The authors declare that they have no conflict of interest. This article does not contain any studies involving animals or human participants performed by any of the authors.
- 5.Akimov S. A., Kuzmin P. I. 2005. The linear tension of the boundary of raft/background monolayer, calculated with account of transverse bending, tilting, and stretching/compression. Biol. membrany (Rus.). 22 (2), 137–146.Google Scholar
- 10.Galimzyanov T.R., Molotkovsky R.J., Kuzmin P.I., Akimov S.A. 2011. Stabilization of bilayer structure of raft due to elastic deformations of membrane. Biochemistry (Moscow) Suppl. Ser. A Membr. Cell. Biol. 5 (3), 286–292.Google Scholar
- 12.Galimzyanov T.R., Molotkovsky R.J., Cohen F.S., Pohl P., Akimov S.A. 2016. Galimzyanov et al. Reply. Phys. Rev. Lett. 116 (7), 079802.Google Scholar
- 29.Akimov S.A., Molotkovsky R.J., Galimzyanov T.R., Radaev A.V., Shilova L.A., Kuzmin P.I., Batishchev O.V., Voronina G.F., Chizmadzhev Y.A. 2014. Model of membrane fusion: Continuous transition to fusion pore with regard of hydrophobic and hydration interactions. Biochemistry (Moscow) Suppl. Ser. A Membr. Cell. Biol. 8 (2), 153–161.Google Scholar
- 31.Akimov S.A., Alexandrova V.V., Galimzyanov T.R., Batishchev O.V. 2017. Interaction of amphipatic peptides mediated by elastic deformations of the membrane. Biol. membrany (Rus.). 34 (3), 162–173.Google Scholar
- 32.Osipenko D.S., Galimzyanov T.R., Akimov S.A. 2016. Lateral redistribution of transmembrane proteins and liquid-ordered domains in lipid membranes with inhomogeneous curvature. Biochemistry (Moscow) Suppl. Ser. A Membr. Cell. Biol. 10 (4), 259–268.Google Scholar
- 35.Worch R., Krupa J., Filipek A., Szymaniec A., Setny P. 2017. Three conserved C-terminal residues of influenza fusion peptide alter its behavior at the membrane interface. Biochim. Biophys. Acta. 1861 (2), 97–105.Google Scholar