The structure of human parvovirus B19

被引:134
作者
Kaufmann, B [1 ]
Simpson, AA [1 ]
Rossmann, MG [1 ]
机构
[1] Purdue Univ, Dept Sci Biol, W Lafayette, IN 47907 USA
关键词
D O I
10.1073/pnas.0402992101
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Human parvovirus B19 is the only parvovirus known to be a human pathogen. The structure of recombinant B19-like particles has been determined to approximate to3.5-Angstrom resolution by x-ray crystallography and, to our knowledge, represents the first near-atomic structure of an Erythrovirus. The polypeptide fold of the major capsid protein VP2 is a "jelly roll" with a beta-barrel motif similar to that found in many icosahedral viruses. The large loops connecting the strands of the beta-barrel form surface features that differentiate B19 from other parvoviruses. Although B19 VP2 has only 26% sequence identity to VP3 of adeno-associated virus, 72% of the C-alpha atoms can be aligned structurally with a rms deviation of 1.8 Angstrom. Both viruses require an integrin as a coreceptor, and conserved surface features suggest a common receptor-binding region.
引用
收藏
页码:11628 / 11633
页数:6
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