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Molecular aspects of the interaction between Mason-Pfizer monkey virus matrix protein and artificial phospholipid

P Junková1, J Prchal2, V Spiwok2

  • 1Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic. junkovap@vscht.cz.

Proteins
|September 1, 2016
PubMed

Insights

The Mason-Pfizer monkey virus matrix protein binds to cell membranes via specific phosphatidylinositol-(4,5)-bisphosphate interactions. Key lysine and tyrosine residues mediate this capsid-membrane binding and protein assembly.

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Mason-Pfizer monkey virus is a type D retrovirus.
  • Retroviral particle assembly occurs in the cytoplasm, followed by transport to the host cell membrane.
  • The matrix protein, N-terminally myristoylated, mediates capsid-membrane association.

Purpose of the Study:

  • To investigate the role of specific amino acid residues in the Mason-Pfizer monkey virus matrix protein's interaction with artificial liposomes.
  • To elucidate the molecular mechanisms underlying capsid-membrane binding and protein oligomerization.

Main Methods:

  • Covalent labeling of arginine, lysine, and tyrosine residues of the matrix protein.
  • Binding studies using artificial liposomes composed of phosphatidylcholine and phosphatidylinositol-(4,5)-bisphosphate (PI(4,5)P2).
  • Multiscale molecular dynamics simulations for interpreting experimental results.

Main Results:

  • Specific PI(4,5)P2 recognition by matrix protein residues K20, K25, K27, K74, and Y28.
  • Residues K92 and K93 stabilize matrix protein orientation on the membrane through PI(4,5)P2 interaction.
  • Residues K33, K39, K54, Y66, Y67, and K87 are involved in matrix protein oligomerization.
  • Arginine residues were accessible, indicating no direct role in membrane interaction or oligomerization.

Conclusions:

  • Identified key residues (K20, K25, K27, K74, Y28) essential for PI(4,5)P2 binding by the Mason-Pfizer monkey virus matrix protein.
  • Elucidated the roles of specific lysine and tyrosine residues in membrane association, protein orientation, and oligomerization.
  • Demonstrated that arginine residues are not directly involved in the capsid-membrane interaction or protein assembly.
Keywords:
covalent labellingliposomesmass spectrometrymultiscale molecular dynamicsphosphatidylinositol-(4,5)-bisphosphateprotein-membrane interaction

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