The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture

Mol Cell. 2005 Apr 15;18(2):161-70. doi: 10.1016/j.molcel.2005.03.019.

Abstract

Comparisons of bacteriophage PRD1 and adenovirus protein structures and virion architectures have been instrumental in unraveling an evolutionary relationship and have led to a proposal of a phylogeny-based virus classification. The structure of the PRD1 spike protein P5 provides further insight into the evolution of viral proteins. The crystallized P5 fragment comprises two structural domains: a globular knob and a fibrous shaft. The head folds into a ten-stranded jelly roll beta barrel, which is structurally related to the tumor necrosis factor (TNF) and the PRD1 coat protein domains. The shaft domain is a structural counterpart to the adenovirus spike shaft. The structural relationships between PRD1, TNF, and adenovirus proteins suggest that the vertex proteins may have originated from an ancestral TNF-like jelly roll coat protein via a combination of gene duplication and deletion.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenoviruses, Human / chemistry
  • Amino Acid Sequence
  • Bacteriophage PRD1 / chemistry*
  • Capsid / chemistry*
  • Capsid Proteins / chemistry*
  • Crystallography, X-Ray
  • Evolution, Molecular*
  • Models, Chemical
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Spectrum Analysis, Raman
  • Tumor Necrosis Factor-alpha / chemistry
  • Viral Proteins / chemistry*

Substances

  • Capsid Proteins
  • Tumor Necrosis Factor-alpha
  • Viral Proteins

Associated data

  • PDB/1YQ5
  • PDB/1YQ6
  • PDB/1YQ8