Publication details
Structure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome Is Packaged via a Pore at a 5-Fold Axis
| Authors | |
|---|---|
| Year of publication | 2011 |
| Type | Article in Periodical |
| Magazine / Source | JOURNAL OF VIROLOGY |
| MU Faculty or unit | |
| Citation | |
| Doi | http://dx.doi.org/10.1128/JVI.02598-10 |
| Field | Microbiology, virology |
| Keywords | VP1 N-TERMINUS; FUNCTIONAL IMPLICATIONS; CANINE PARVOVIRUS; DNA-REPLICATION; TYPE-2; PROTEIN; HELICASE; BINDING; CAPSIDS; VIRION |
| Description | The parvovirus minute virus of mice (MVM) packages a single copy of its linear single-stranded DNA genome into preformed capsids, in a process that is probably driven by a virus-encoded helicase. Parvoviruses have a roughly cylindrically shaped pore that surrounds each of the 12 5-fold vertices. The pore, which penetrates the virion shell, is created by the juxtaposition of 10 antiparallel beta-strands, two from each of the 5-fold-related capsid proteins. There is a bottleneck in the channel formed by the symmetry-related side chains of the leucines at position 172. We report here the X-ray crystal structure of the particles produced by a leucine-to-tryptophan mutation at position 172 and the analysis of its biochemical properties. The mutant capsid had its 5-fold channel blocked, and the particles were unable to package DNA, strongly suggesting that the 5-fold pore is the packaging portal for genome entry. |