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Originally published In Press as doi:10.1074/jbc.M208691200 on January 30, 2003

J. Biol. Chem., Vol. 278, Issue 14, 12546-12553, April 4, 2003
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Interaction of L2 with beta -Actin Directs Intracellular Transport of Papillomavirus and Infection*

Rongcun YangDagger , William H. Yutzy IVDagger , Raphael P. Viscidi§, and Richard B. S. RodenDagger ||

From the Departments of Dagger  Pathology, § Pediatrics, and  Gynecology and Obstetrics, The Johns Hopkins School of Medicine, Baltimore, Maryland 21205

Viruses that replicate in the nucleus, including the primary causative agent of cervical cancer, human papillomavirus type 16 (HPV16), must first cross the cytoplasm. We compared the uptake of HPV16 virus-like particles (VLPs) either with or without the minor capsid protein L2. Whereas VLPs containing only the major capsid protein L1 were diffusely distributed within the cytoplasm even 6 h post-infection, VLPs comprising both L1 and L2 exhibited a radial distribution in the cytoplasm and accumulated in the perinuclear region of BPHE-1 cells within 2 h. L2 of HPV16 or bovine papillomavirus was shown to bind to a 43-kDa cellular protein that was subsequently identified as beta -actin by matrix-assisted laser desorption ionization time-of-flight analysis. A conserved domain comprising residues 25-45 of HPV16 L2 was sufficient for interaction with beta -actin. HPV16 L2 residues 25-45 fused to green fluorescent protein, but not green fluorescent protein alone, colocalized with actin and caused cell retraction and disruption of the microfilament network. Finally, wild-type L2, but not L2 with residues 25-45 deleted, facilitated HPV16 pseudovirion infection. Thus, binding of beta -actin by L2 residues 25-45 facilitates transport of HPV16 across the cytoplasm during infection, and blockade of this novel interaction may be useful for prophylaxis.

* This work was supported by Grants AI48203 and CA83706 from the National Institutes of Health the Cancer Research Institute, and by American Cancer Society Grant RSG MBC-103111 (to R. B. S. R.). The work performed at the Mass Spectrometry Facility of The Johns Hopkins School of Medicine was supported by National Center for Research Resources Shared Instrumentation Grant 1S10-RR14702 and the Johns Hopkins Fund for Medical Discovery.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Pathology, The Johns Hopkins School of Medicine, Ross 512B, 720 Rutland Ave., Baltimore, MD 21205. Tel.: 410-502-5161; Fax: 443-287-4295; E-mail: roden@jhmi.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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