The Structure of Human Parvovirus B19

• Published in: Proceedings of the National Academy of Sciences - PNAS 2004-08, Vol.101 (32), p.11628-11633
• Main Authors: Kaufmann, Bärbel, Simpson, Alan A., Rossmann, Michael G., Petsko, Gregory A.
• Format: Article
• Language: English
• Subjects: Amino acids; Atoms; Biological Sciences; Biophysics; Canyons; Capsid; Capsid Proteins - chemistry; Crystallography; Crystallography, X-Ray; Crystals; Erythrovirus; Human parvovirus B19; Humans; Immunodominant epitopes; Models, Molecular; Parvovirus; Parvovirus B19, Human - chemistry; Pathogens; Protein Conformation; Proteins; Sequence Alignment; Surface Properties; Virion - chemistry; Viruses
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.0402992101

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 Cαatoms 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.