The structure of human parvovirus B19
- Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907-2054
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Edited by Gregory A. Petsko, Brandeis University, Waltham, MA, and approved June 28, 2004 (received for review April 28, 2004)
Abstract
Human parvovirus B19 is the only parvovirus known to be a human pathogen. The structure of recombinant B19-like particles has been determined to ≈3.5-Å 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 β-barrel motif similar to that found in many icosahedral viruses. The large loops connecting the strands of the β-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 Cα atoms can be aligned structurally with a rms deviation of 1.8 Å. Both viruses require an integrin as a coreceptor, and conserved surface features suggest a common receptor-binding region.
Footnotes
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↵ † To whom correspondence should be addressed. E-mail: mgr{at}indiana.bio.purdue.edu.
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↵ * Present address: Stroma, Disblair Road, AB21 0PU Newmachar, Scotland.
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This paper was submitted directly (Track II) to the PNAS office.
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Abbreviations: RMSD, rms deviation; SPV, simian parvovirus; PtPV, pig-tailed macaque parvovirus; RhPV, rhesus macaque parvovirus; AAV-2, adeno-associated virus 2; FPV, feline panleukopenia virus.
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Data deposition: The atomic coordinates and structure factors have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 1S58).
- Copyright © 2004, The National Academy of Sciences
