文章基本信息

标题：The structure of human parvovirus B19
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作者：Bärbel Kaufmann ; Alan A. Simpson ; Michael G. Rossmann 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2004
卷号：101
期号：32
页码：11628-11633
DOI：10.1073/pnas.0402992101
语种：English
出版社：The National Academy of Sciences of the United States of America
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 {approx}3.5-A 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 A. Both viruses require an integrin as a coreceptor, and conserved surface features suggest a common receptor-binding region.