Kaufmann, Baerbel and Chipman, Paul R. and Kostyuchenko, Victor A. and Modrow, Susanne and Rossmann, Michael G. (2008) Visualization of the externalized VP2N termini of infectious human parvovirus B19. JOURNAL OF VIROLOGY, 82 (15). pp. 7306-7312. ISSN 0022-538X, 1098-5514
Full text not available from this repository. (Request a copy)Abstract
The structures of infectious human parvovirus B19 and empty wild-type particles were determined by cryoelectron microscopy (cryoEM) to 7.5-angstrom and 11.3 angstrom resolution, respectively, assuming icosahedral symmetry. Both of these, DNA filled and empty, wild-type particles contain a few copies of the minor capsid protein VP1 Comparison of wild-type B19 with the crystal structure and cryoEM reconstruction of recombinant B19 particles consisting of only the major capsid protein VP2 showed structural differences in the vicinity of the icosahedral fivefold axes. Although the unique N-terminal region of VP1 could not be visualized in the icosahedrally averaged maps, the N terminus of VP2 was shown to be exposed on the viral surface adjacent to the fivefold beta-cylinder. The conserved glycine-rich region is positioned between two neighboring, fivefold-symmetrically related VP subunits and not in the fivefold channel as observed for other parvoviruses.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MINOR CAPSID PROTEIN; VIRUS TYPE-2 CAPSIDS; VP1 N-TERMINUS; MINUTE VIRUS; CANINE PARVOVIRUS; UNIQUE REGION; STRUCTURAL POLYPEPTIDES; FUNCTIONAL IMPLICATIONS; VP1N-TERMINAL SEQUENCE; ANGSTROM RESOLUTION; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 27 Oct 2020 12:26 |
| Last Modified: | 27 Oct 2020 12:26 |
| URI: | https://pred.uni-regensburg.de/id/eprint/30547 |
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