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

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.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Merckel MC,Huiskonen JT,Bamford DH,Goldman A,Tuma R

doi

10.1016/j.molcel.2005.03.019

subject

Has Abstract

pub_date

2005-04-15 00:00:00

pages

161-70

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(05)01189-5

journal_volume

18

pub_type

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