PLEVKA, Pavel, Susan HAFENSTEIN, Lei LI, Anthony, Jr. D'ABRAMO, Susan F. COTMORE, Michael G. ROSSMANN and Peter TATTERSALL. 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. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2011, vol. 85, No 10, p. 4822-4827. ISSN 0022-538X. Available from: https://dx.doi.org/10.1128/JVI.02598-10.
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Basic information
Original name 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 PLEVKA, Pavel, Susan HAFENSTEIN, Lei LI, Anthony, Jr. D'ABRAMO, Susan F. COTMORE, Michael G. ROSSMANN and Peter TATTERSALL.
Edition JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2011, 0022-538X.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 5.402
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1128/JVI.02598-10
UT WoS 000289787300019
Keywords in English VP1 N-TERMINUS; FUNCTIONAL IMPLICATIONS; CANINE PARVOVIRUS; DNA-REPLICATION; TYPE-2; PROTEIN; HELICASE; BINDING; CAPSIDS; VIRION
Tags neMU
Changed by Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 29/3/2017 14:59.
Abstract
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.
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