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J Virol, July 1998, p. 6186-6189, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Papillomavirus Assembly Requires Trimerization of the Major Capsid Protein by Disulfides between Two Highly Conserved Cysteines

Martin Sapp,1,* Claudia Fligge,1 Ingrid Petzak,1 J. Robin Harris,2 and Rolf E. Streeck1

Institute for Medical Microbiology and Hygiene1 and Institute of Zoology,2 University of Mainz, D-55101 Mainz, Germany

Received 22 January 1998/Accepted 1 April 1998

We have used viruslike particles (VLPs) of human papillomaviruses to study the structure and assembly of the viral capsid. We demonstrate that mutation of either of two highly conserved cysteines of the major capsid protein L1 to serine completely prevents the assembly of VLPs but not of capsomers, whereas mutation of all other cysteines leaves VLP assembly unaffected. These two cysteines form intercapsomeric disulfides yielding an L1 trimer. Trimerization comprises about half of the L1 molecules in VLPs but all L1 molecules in complete virions. We suggest that trimerization of L1 is indispensable for the stabilization of intercapsomeric contacts in papillomavirus capsids.

* Corresponding author. Mailing address: Institute for Medical Microbiology and Hygiene, Johannes-Gutenberg-Universität Mainz, Hochhaus am Augustusplatz, D-55101 Mainz, Germany. Phone: 49-6131-175135. Fax: 49-6131-392359. E-mail: sapp{at}goofy.zdv.uni-mainz.de.

J Virol, July 1998, p. 6186-6189, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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Copyright © 1998 by the American Society for Microbiology. All rights reserved.