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Visualization of the externalized VP2 N termini of infectious human parvovirus B19

Bärbel Kaufmann1, Paul R Chipman, Victor A Kostyuchenko

  • 1Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907-2054, USA.

Journal of Virology
|May 30, 2008
PubMed

Insights

Structural analysis of human parvovirus B19 using cryoelectron microscopy revealed key differences in capsid protein arrangements. These findings offer insights into parvovirus structure and assembly.

Area of Science:

  • Structural biology
  • Virology
  • Biophysics

Background:

  • Human parvovirus B19 is a significant human pathogen.
  • Understanding parvovirus structure is crucial for developing antiviral strategies.

Purpose of the Study:

  • To determine the high-resolution structures of infectious and empty human parvovirus B19 particles.
  • To compare the structures of wild-type B19 with recombinant VP2-only particles.

Main Methods:

  • Cryoelectron microscopy (cryoEM) was used to determine structures.
  • Icosahedral symmetry was assumed for reconstructions.
  • Structures were resolved to 7.5-A and 11.3-A for filled and empty particles, respectively.

Main Results:

  • Both DNA-filled and empty wild-type B19 particles contain minor capsid protein VP1.
  • Structural differences were observed near the fivefold axes when comparing wild-type B19 with VP2-only particles.
  • The N terminus of VP2 is exposed on the viral surface, and the glycine-rich region is positioned between VP subunits.

Conclusions:

  • The study provides detailed structural insights into human parvovirus B19.
  • Differences in VP1 and VP2 arrangement impact viral structure.
  • Findings contribute to understanding parvovirus assembly and evolution.

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