Tale of two spikes in bacteriophage PRD1.
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...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2007
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| _version_ | 1797071486527209472 |
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| author | Huiskonen, J Manole, V Butcher, S |
| author_facet | Huiskonen, J Manole, V Butcher, S |
| author_sort | Huiskonen, J |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T22:53:58Z |
| format | Journal article |
| id | oxford-uuid:5fc04a40-24ad-4ed0-b060-57acf615019f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:53:58Z |
| publishDate | 2007 |
| record_format | dspace |
| spelling | oxford-uuid:5fc04a40-24ad-4ed0-b060-57acf615019f2022-03-26T17:48:52ZTale of two spikes in bacteriophage PRD1.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:5fc04a40-24ad-4ed0-b060-57acf615019fEnglishSymplectic Elements at Oxford2007Huiskonen, JManole, VButcher, SStructural 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. |
| spellingShingle | Huiskonen, J Manole, V Butcher, S Tale of two spikes in bacteriophage PRD1. |
| title | Tale of two spikes in bacteriophage PRD1. |
| title_full | Tale of two spikes in bacteriophage PRD1. |
| title_fullStr | Tale of two spikes in bacteriophage PRD1. |
| title_full_unstemmed | Tale of two spikes in bacteriophage PRD1. |
| title_short | Tale of two spikes in bacteriophage PRD1. |
| title_sort | tale of two spikes in bacteriophage prd1 |
| work_keys_str_mv | AT huiskonenj taleoftwospikesinbacteriophageprd1 AT manolev taleoftwospikesinbacteriophageprd1 AT butchers taleoftwospikesinbacteriophageprd1 |