Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 101, Issue 32, Pages 11628-11633Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0402992101
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- NIAID NIH HHS [AI11219, R01 AI011219, R37 AI011219] Funding Source: Medline
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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.
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