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Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures

S D Benson1, J K Bamford, D H Bamford

  • 1The Wistar Institute, Philadelphia, Pennsylvania 19104, USA.

Cell
|September 28, 1999
PubMed

Insights

Bacteriophage PRD1

Area of Science:

  • Structural biology
  • Virology
  • Evolutionary biology

Background:

  • Bacteriophage PRD1 possesses a unique internal membrane within its icosahedral protein shell.
  • The major coat protein (P3) of PRD1 is crucial for capsid structure and stability.

Purpose of the Study:

  • To determine the high-resolution crystal structure of the PRD1 major coat protein (P3).
  • To investigate the structural similarities between PRD1 and human adenovirus, despite infecting different hosts.

Main Methods:

  • X-ray crystallography at 1.85 A resolution.
  • Comparative structural analysis of viral coat proteins and capsid architecture.

Main Results:

  • The crystal structure of P3 revealed a trimeric molecule with eight-stranded viral jelly roll motifs.
  • P3 shares significant structural homology with hexon, the major coat protein of human adenovirus.
  • PRD1 and adenovirus exhibit similar overall architectures, including capsid lattices and vertex proteins.

Conclusions:

  • The striking structural similarities suggest a shared evolutionary origin between bacteriophage PRD1 and human adenovirus.
  • This finding provides insights into the evolution of double-stranded DNA (dsDNA) viruses across different host kingdoms.

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