Abstrakti
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.
Alkuperäiskieli | englanti |
---|---|
Lehti | Proceedings of the National Academy of Sciences of the United States of America |
Vuosikerta | 104 |
Numero | 16 |
Sivut | 6666-6671 |
Sivumäärä | 6 |
ISSN | 0027-8424 |
DOI - pysyväislinkit | |
Tila | Julkaistu - 2007 |
OKM-julkaisutyyppi | A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä, vertaisarvioitu |
Tieteenalat
- 118 Biotieteet