Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore complex promote virus infection.

作者: Sten Strunze , Martin F. Engelke , I-Hsuan Wang , Daniel Puntener , Karin Boucke

DOI: 10.1016/J.CHOM.2011.08.010

关键词:

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

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