Three-dimensional structure and function of the Paramecium bursaria chlorella virus capsid

Xinzheng Zhang, Ye Xiang, David D. Dunigan, Thomas Klose, Paul R. Chipman, James L. Van Etten, Michael G. Rossmann

Research output: Contribution to journalArticlepeer-review

62 Scopus citations


A cryoelectron microscopy 8.5 Å resolution map of the 1,900 Å diameter, icosahedral, internally enveloped Paramecium bursaria chlorella virus was used to interpret structures of the virus at initial stages of cell infection. A fivefold averaged map demonstrated that two minor capsid proteins involved in stabilizing the capsid are missing in the vicinity of the unique vertex. Reconstruction of the virus in the presence of host chlorella cell walls established that the spike at the unique vertex initiates binding to the cell wall, which results in the enveloped nucleocapsid moving closer to the cell. This process is concurrent with the release of the internal viral membrane that was linked to the capsid by many copies of a viral membrane protein in the mature infectous virus. Simultaneously, part of the trisymmetrons around the unique vertex disassemble, probably in part because two minor capsid proteins are absent, causing Paramecium bursaria chlorella virus and the cellular contents to merge, possibly as a result of enzyme(s) within the spike assembly. This may be one of only a few recordings of successive stages of a virus while infecting a eukaryotic host in pseudoatomic detail in three dimensions.

Original languageEnglish (US)
Pages (from-to)14837-14842
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number36
StatePublished - Sep 6 2011
Externally publishedYes


  • 3D structure
  • Cell entry
  • Conformation changes
  • Minor proteins
  • PBCV-1

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Three-dimensional structure and function of the Paramecium bursaria chlorella virus capsid'. Together they form a unique fingerprint.

Cite this