Structural comparisons between bacteriophage PRD1 and adenovirus have revealed an evolutionary relationship that has contributed significantly to current ideas on virus phylogeny. However, the structural organization of the receptor-binding spike complex and how the different symmetry mismatches are mediated between the spike-complex proteins are not clear. We determined the architecture of the PRD1 spike complex by using electron microscopy and three-dimensional image reconstruction of a series of PRD1 mutants. We constructed an atomic model for the full-length P5 spike protein by using comparative modeling. P5 was shown to be bound directly to the penton base protein P31. P5 and the receptor-binding protein P2 form two separate spikes, interacting with each other near the capsid shell. P5, with a tumor necrosis factor-like head domain, may have been responsible for host recognition before capture of the current receptor-binding protein P2.
|Lehti||Proceedings of the National Academy of Sciences of the United States of America|
|DOI - pysyväislinkit|
|Tila||Julkaistu - 2007|
|OKM-julkaisutyyppi||A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä, vertaisarvioitu|
- 118 Biotieteet