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First published online 8 December 2005
doi: 10.1242/jcs.02705
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Research Article |
1 Institute of Physiology II, University of Münster, Robert-Koch-Str. 27b, 48149 Münster, Germany
2 Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK
3 Institute of Medical Microbiology, University of Münster, Domagkstr. 10, 48149 Münster, Germany
4 Interdisciplinary Center of Clinical Research (IZKF), Domagkstr. 3, 48149 Münster, Germany
* Author for correspondence (e-mail: vs297{at}cam.ac.uk)
Accepted 21 September 2005
Incoming herpes simplex virus type-1 (HSV-1) capsids are known to dock to the nuclear pore complex (NPC) and release their genome. It has remained elusive, however, how the huge viral DNA translocates through the comparatively small NPC channel. In the present study, the interaction of HSV-1 with NPCs was analyzed by atomic force microscopy. In addition to capsids, smaller subviral structures - most with a diameter of 35-40 nm and a length of 130-160 nm - were visualized at the cytoplasmic side of the NPC. These components differed from capsids in their adhesion and stiffness properties, and were the sole subviral structures translocated through dilated NPCs towards the nucleus. It is presumed that they are the HSV-1 genome, and that a change in NPC conformation allows translocation of this genome as a densely packaged, rodlike structure.
Key words: Atomic force microscopy, Herpes simplex virus type-1, Viral genome, Nuclear import, Nuclear pore complex
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