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Related Experiment Videos

Solution structure of bacteriophage PRD1 vertex complex.

A Sokolova1, M Malfois, J Caldentey

  • 1Institute of Crystallography, Russian Academy of Sciences, Moscow 117333, Russia.

The Journal of Biological Chemistry
|September 29, 2001
PubMed
Summary

Bacteriophage PRD1 and adenovirus share structural similarities, but their vertex protein assemblies differ. This study reveals distinct quaternary structures of PRD1

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Area of Science:

  • Structural biology
  • Virology
  • Biochemistry

Background:

  • Bacteriophage PRD1 is a model virus with an internal membrane and icosahedral capsid.
  • PRD1 shares structural similarities with adenovirus, particularly in their major coat proteins.
  • The 5-fold vertex assemblies of these viruses are crucial for host cell interaction and DNA delivery.

Purpose of the Study:

  • To investigate the structural similarities and differences between bacteriophage PRD1 and adenovirus vertex assemblies.
  • To elucidate the quaternary structures and interactions of PRD1's vertex proteins (P2, P5, and P31).

Main Methods:

  • Synchrotron radiation x-ray solution scattering was employed to study purified PRD1 spike proteins.
  • Ab initio low-resolution models of vertex proteins P5, P2, and P31 were reconstructed from scattering data.

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Main Results:

  • Protein P5 forms a long trimer, analogous to adenovirus spike protein pIV.
  • Receptor-binding protein P2 is a unique monomer without an adenovirus counterpart.
  • P31 forms a thinner pentameric base than adenovirus penton pIII, and P5 can form nonameric or P5(6):P31 complexes.

Conclusions:

  • The study provides models supporting vertex assembly in bacteriophage PRD1.
  • Despite overall architectural similarities, significant differences exist between PRD1 and adenovirus spike assemblies.