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Journal of Virology, June 2005, p. 6723-6731, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6723-6731.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Interaction of tSNARE Syntaxin 18 with the Papillomavirus Minor Capsid Protein Mediates Infection

Ioannis Bossis,1 Richard B. S. Roden,1,2,3 Ratish Gambhira,1 Rongcun Yang,1 Mitsuo Tagaya,4 Peter M. Howley,5 and Patricio I. Meneses5,6*

Departments of Pathology,1 Oncology,2 Gynecology and Obstetrics, John Hopkins University, Baltimore, Maryland 21205,3 School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo, Japan 192-0392,4 Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115,5 Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 191046

Received 13 December 2004/ Accepted 25 January 2005

The papillomavirus capsid mediates binding to the cell surface and passage of the virion to the perinuclear region during infection. To better understand how the virus traffics across the cell, we sought to identify cellular proteins that bind to the minor capsid protein L2. We have identified syntaxin 18 as a protein that interacts with bovine papillomavirus type 1 (BPV1) L2. Syntaxin 18 is a target membrane-associated soluble N-ethylmaleimide-sensitive factor-attachment protein receptor (tSNARE) that resides in the endoplasmic reticulum (ER). The ectopic expression of FLAG-tagged syntaxin 18, which disrupts ER trafficking, blocked BPV1 pseudovirion infection. Furthermore, the expression of FLAG-syntaxin 18 prevented the passage of BPV1 pseudovirions to the perinuclear region that is consistent with the ER. Genetic studies identified a highly conserved L2 domain, DKILK, comprising residues 40 to 44 that mediated BPV1 trafficking through the ER during infection via an interaction with the tSNARE syntaxin 18. Mutations within the DKILK motif of L2 that did not significantly impact virion morphogenesis or binding at the cell surface prevented the L2 interaction with syntaxin 18 and disrupted BPV1 infection.

* Corresponding author. Mailing address: Department of Microbiology, University of Pennsylvania School of Medicine, 202A Johnson Pavilion, 3610 Hamilton Walk, Philadelphia, PA 19104. Phone: (215) 746-0116. Fax: (215) 898-9557. E-mail: pmeneses{at}mail.med.upenn.edu.

Journal of Virology, June 2005, p. 6723-6731, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6723-6731.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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