Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures

被引:241
作者
Benson, SD
Bamford, JKH
Bamford, DH
Burnett, RM
机构
[1] Wistar Inst Anat & Biol, Philadelphia, PA 19104 USA
[2] Univ Helsinki, Inst Biotechnol, FIN-00014 Helsinki, Finland
[3] Univ Helsinki, Dept Biosci, FIN-00014 Helsinki, Finland
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
D O I
10.1016/S0092-8674(00)81516-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The unusual bacteriophage PRD1 features a membrane beneath its icosahedral protein coat. The crystal structure of the major coat protein, P3, at 1.85 Angstrom resolution reveals a molecule with three interlocking subunits, each with two eight-stranded viral jelly rolls normal to the viral capsid, and putative membrane-interacting regions. Surprisingly, the P3 molecule closely resembles hexon, the equivalent protein in human adenovirus. Both viruses also have similar overall architecture, with identical capsid lattices and attachment proteins at their vertices. Although these two dsDNA viruses infect hosts from very different kingdoms, their striking similarities, from major coat protein through capsid architecture, strongly suggest their evolutionary relationship.
引用
收藏
页码:825 / 833
页数:9
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