title: Molecular aspects of the interaction between Mason-Pfizer monkey virus matrix protein and artificial phospholipid membrane.
abstract: The Mason-Pfizer monkey virus is a type D retrovirus, which assembles its immature particles in the cytoplasm prior to their transport to the host cell membrane. The association with the membrane is mediated by the N-terminally myristoylated matrix protein. To reveal the role of particular residues which are involved in the capsid-membrane interaction, covalent labelling of arginine, lysine and tyrosine residues of the Mason-Pfizer monkey virus matrix protein bound to artificial liposomes containing 95% of phosphatidylcholine and 5% phosphatidylinositol-(4,5)-bisphosphate (PI(4,5)P2) was performed. The experimental results were interpreted by multiscale molecular dynamics simulations. The application of these two complementary approaches helped us to reveal that matrix protein specifically recognizes the PI(4,5)P2molecule by the residues K20, K25, K27, K74, and Y28, while the residues K92 and K93 stabilizes the matrix protein orientation on the membrane by the interaction with another PI(4,5)P2molecule. Residues K33, K39, K54, Y66, Y67, and K87 appear to be involved in the matrix protein oligomerization. All arginine residues remained accessible during the interaction with liposomes which indicates that they neither contribute to the interaction with membrane nor are involved in protein oligomerization. Proteins 2016; 84:1717-1727. © 2016 Wiley Periodicals, Inc.
authors: Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic. junkovap@vscht.cz.
authors: P
authors: P
authors: Junková
authors: Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.
authors: J
authors: J
authors: Prchal
authors: Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.
authors: V
authors: V
authors: Spiwok
authors: Laboratory of Cell Biology, Institute of Experimental Botany, Academy of Sciences of the Czech Republic, Prague, Czech Republic.|Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
authors: R
authors: R
authors: Pleskot
authors: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
authors: J
authors: J
authors: Kadlec
authors: Laboratory of molecular structure characterisation, Institute of Microbiology of the ASCR, Academy of Sciences of the Czech Republic, Prague, Czech Republic.|Department of Cancer Biology, Institute of Cancer Research, London, United Kingdom.
authors: L
authors: L
authors: Krásný
authors: Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.
authors: R
authors: R
authors: Hynek
authors: Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.
authors: R
authors: R
authors: Hrabal
authors: Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.
authors: T
authors: T
authors: Ruml
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry*; D016093:Mason-Pfizer monkey virus / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry; D010713:Phosphatidylcholines / Q000737:chemistry; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000737:chemistry; D011485:Protein Binding; D013194:Staining and Labeling; D014443:Tyrosine / Q000737:chemistry*; D014763:Viral Matrix Proteins / Q000737:chemistry*
chemical_list: D008081:Liposomes; D010455:Peptides; D010713:Phosphatidylcholines; D019269:Phosphatidylinositol 4,5-Diphosphate; D014763:Viral Matrix Proteins; D014443:Tyrosine; D001120:Arginine; D008239:Lysine
keywords: covalent labelling; liposomes; mass spectrometry; multiscale molecular dynamics; phosphatidylinositol-(4,5)-bisphosphate; protein-membrane interaction