The structure of human parvovirus B19.
Human parvovirus B19 is the only parvovirus known to be a human pathogen. The structure of recombinant B19-like particles has been determined to approximately 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.
Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907-2054, USA.
Bärbel
B
Kaufmann
Alan A
AA
Simpson
Michael G
MG
Rossmann
D036022:Capsid Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D016732:Parvovirus B19, Human / Q000737:chemistry*; D011487:Protein Conformation; D016415:Sequence Alignment; D013499:Surface Properties; D014771:Virion / Q000737:chemistry
D036022:Capsid Proteins; C095548:capsid protein VP2, parvovirus B19