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Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization

Zdenĕk Knejzlík1, Pavel Ulbrich, Martin Strohalm

  • 1Department of Biochemistry and Microbiology, Institute of Chemical Technology, Technická 5, 166 28 Prague 6, Czech Republic.

Virology
|August 25, 2009
PubMed

Insights

The Mason-Pfizer monkey virus Gag p12 domain fragment forms fibers through a concentration-dependent process. This assembly involves a conformational change to alpha-helix structures during multimerization, clarifying Gag-Gag interactions.

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Mason-Pfizer monkey virus is a Betaretrovirus.
  • Gag polyprotein precursors assemble immature viral particles.
  • The N-terminal Gag p12 domain is crucial for efficient assembly, but its role in Gag-Gag interactions is unclear.

Purpose of the Study:

  • To investigate the precise role of the Gag p12 domain in mediating Gag-Gag interactions.
  • To elucidate the structural mechanisms underlying Gag particle assembly.

Main Methods:

  • Recombinant wt-Np12 protein prepared by in vitro transcription and translation.
  • Circular dichroism spectroscopy.
  • Electron microscopy.
  • Ultracentrifugation analyses.

Main Results:

  • The wt-Np12 domain fragment self-assembles into fibrillar structures.
  • Fiber formation is concentration-dependent.
  • Assembly is associated with a conformational transition from an unfolded/non-periodical state to an alpha-helical structure during multimerization.

Conclusions:

  • The Gag p12 domain plays a critical role in viral assembly through concentration-dependent fibril formation.
  • Multimerization of p12 involves a significant conformational change, contributing to Gag-Gag interactions and particle assembly.

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