Molecular aspects of the interaction between Mason-Pfizer monkey virus matrix protein and artificial phospholipid membrane
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
27578150
DOI
10.1002/prot.25156
Knihovny.cz E-zdroje
- Klíčová slova
- covalent labelling, liposomes, mass spectrometry, multiscale molecular dynamics, phosphatidylinositol-(4,5)-bisphosphate, protein-membrane interaction,
- MeSH
- arginin chemie MeSH
- barvení a značení MeSH
- fosfatidylcholiny chemie MeSH
- fosfatidylinositol-4,5-difosfát chemie MeSH
- liposomy chemie MeSH
- lysin chemie MeSH
- Masonův-Pfizerův opičí virus chemie MeSH
- peptidy chemie MeSH
- proteiny virové matrix chemie MeSH
- sekvence aminokyselin MeSH
- simulace molekulární dynamiky MeSH
- tyrosin chemie MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- arginin MeSH
- fosfatidylcholiny MeSH
- fosfatidylinositol-4,5-difosfát MeSH
- liposomy MeSH
- lysin MeSH
- peptidy MeSH
- proteiny virové matrix MeSH
- tyrosin MeSH
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)P2 molecule 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)P2 molecule. 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.
Citace poskytuje Crossref.org
Interaction Interface of Mason-Pfizer Monkey Virus Matrix and Envelope Proteins
