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Journal of Virology, July 2006, p. 6691-6696, Vol. 80, No. 13
0022-538X/06/$08.00+0 doi:10.1128/JVI.00057-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Institute for Medical Microbiology and Hygiene,1 First Department of Internal Medicine, Johannes Gutenberg University, Mainz, Germany,2 Department of Microbiology and Immunology,3 Center for Molecular and Tumor Virology,4 Feist-Weiller Cancer Center, LSU Health Sciences Center, Shreveport, Louisiana5
Received 9 January 2006/ Accepted 6 April 2006
Papillomaviruses enter cells via endocytosis (H. C. Selinka et al., Virology 299:279-287, 2002). After egress from endosomes, the minor capsid protein L2 accompanies the viral DNA to the nucleus and subsequently to the subnuclear promyelocytic leukemia protein bodies (P. M. Day et al., Proc. Natl. Acad. Sci. USA 101:14252-14257, 2004), suggesting that this protein may be involved in the intracytoplasmic transport of the viral genome. We now demonstrate that the L2 protein is able to interact with the microtubule network via the motor protein dynein. L2 protein was found attached to microtubules after uncoating of incoming human papillomavirus pseudovirions. Based on immunofluorescence and coimmunoprecipitation analyses, the L2 region interacting with dynein is mapped to the C-terminal 40 amino acids. Mutations within this region abrogating the L2/dynein interaction strongly reduce the infectivity of pseudoviruses, indicating that this interaction mediates the minus-end-directed transport of the viral genome along microtubules towards the nucleus.
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