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Journal of Virology, December 2008, p. 12565-12568, Vol. 82, No. 24
0022-538X/08/$08.00+0 doi:10.1128/JVI.01631-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Laboratory of Cellular Oncology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland
Received 30 July 2008/ Accepted 23 September 2008
Papillomavirus infection normally involves virion binding to cell surface heparan sulfate proteoglycans (HSPGs). However, we found that human papillomavirus type 16 pseudovirions efficiently bound and infected cells lacking HSPGs if their L2 capsid protein was precleaved by furin, a cellular protease required for infection. The inability of pseudovirions to efficiently bind and infect cultured primary keratinocytes was also overcome by furin precleavage, suggesting that the defect involves altered HSPG modification. We conclude that the primary function of HSPG binding is to enable cell surface furin cleavage of L2 and that binding to a distinct cell surface receptor(s) is a subsequent step of papillomavirus infection.
Published ahead of print on 1 October 2008.
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