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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-49885

Strunze, S; Engelke, M F; Wang, I-H; Puntener, D; Boucke, K; Schleich, S; Way, M; Schoenenberger, P; Burckhardt, C J; Greber, U F (2011). Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore complex promote virus infection. Cell Host & Microbe, 10(3):210-223.

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Abstract

Many viruses deliver their genomes into the host cell nucleus for replication. However, the size restrictions of the nuclear pore complex (NPC), which regulates the passage of proteins, nucleic acids, and solutes through the nuclear envelope, require virus capsid uncoating before viral DNA can access the nucleus. We report a microtubule motor kinesin-1-mediated and NPC-supported mechanism of adenovirus uncoating. The capsid binds to the NPC filament protein Nup214 and kinesin-1 light-chain Klc1/2. The nucleoporin Nup358, which is bound to Nup214/Nup88, interacts with the kinesin-1 heavy-chain Kif5c to indirectly link the capsid to the kinesin motor. Kinesin-1 disrupts capsids docked at Nup214, which compromises the NPC and dislocates nucleoporins and capsid fragments into the cytoplasm. NPC disruption increases nuclear envelope permeability as indicated by the nuclear influx of large cytoplasmic dextran polymers. Thus, kinesin-1 uncoats viral DNA and compromises NPC integrity, allowing viral genomes nuclear access to promote infection.

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29 citations in Web of Science®
30 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Institute of Molecular Life Sciences
DDC:570 Life sciences; biology
Uncontrolled Keywords:kinesin; DNA tumor virus; nuclear pore complex; Nup214; Nup358; nuclear import; virus uncoating; disassembly; microtubule; motor protein; DNA import; nuclear transport; heavy chain; light chain; protein IX;
Language:English
Date:15 September 2011
Deposited On:10 Oct 2011 15:33
Last Modified:30 Nov 2013 01:21
Publisher:Elsevier
ISSN:1931-3128
Publisher DOI:10.1016/j.chom.2011.08.010
PubMed ID:21925109

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