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Journal of Virology, June 2008, p. 5190-5197, Vol. 82, No. 11
0022-538X/08/$08.00+0     doi:10.1128/JVI.02726-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Arrangement of L2 within the Papillomavirus Capsid{triangledown}

Christopher B. Buck,1 Naiqian Cheng,2 Cynthia D. Thompson,1 Douglas R. Lowy,1 Alasdair C. Steven,2 John T. Schiller,1 and Benes L. Trus2,3*

Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland 20892,1 Laboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, NIH, Bethesda, Maryland 20892,2 Imaging Sciences Laboratory, Center for Information Technology, and National Institute of Arthritis, Musculoskeletal and Skin Diseases, NIH, Bethesda, Maryland, 208923

Received 21 December 2007/ Accepted 15 March 2008

Papillomaviruses are a family of nonenveloped DNA tumor viruses. Some sexually transmitted human papillomavirus (HPV) types, including HPV type 16 (HPV16), cause cancer of the uterine cervix. Papillomaviruses encode two capsid proteins, L1 and L2. The major capsid protein, L1, can assemble spontaneously into a 72-pentamer icosahedral structure that closely resembles native virions. Although the minor capsid protein, L2, is not required for capsid formation, it is thought to participate in encapsidation of the viral genome and plays a number of essential roles in the viral infectious entry pathway. The abundance of L2 and its arrangement within the virion remain unclear. To address these questions, we developed methods for serial propagation of infectious HPV16 capsids (pseudoviruses) in cultured human cell lines. Biochemical analysis of capsid preparations produced using various methods showed that up to 72 molecules of L2 can be incorporated per capsid. Cryoelectron microscopy and image reconstruction analysis of purified capsids revealed an icosahedrally ordered L2-specific density beneath the axial lumen of each L1 capsomer. The relatively close proximity of these L2 density buttons to one another raised the possibility of homotypic L2 interactions within assembled virions. The concept that the N and C termini of neighboring L2 molecules can be closely apposed within the capsid was supported using bimolecular fluorescence complementation or "split GFP" technology. This structural information should facilitate investigation of L2 function during the assembly and entry phases of the papillomavirus life cycle.

* Corresponding author. Mailing address: National Institutes of Health, 12 Center Drive, MSC 5624, Bethesda, MD 20892-5624. Phone: (301) 496-2250. Fax: (301) 402-2867. E-mail: Benes_Trus{at}nih.gov

{triangledown} Published ahead of print on 26 March 2008.

Journal of Virology, June 2008, p. 5190-5197, Vol. 82, No. 11
0022-538X/08/$08.00+0     doi:10.1128/JVI.02726-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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