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1 Institut für Medizinische Mikrobiologie, Johannes-Gutenberg-Universität Mainz, Hochhaus am Augustusplatz, D-55101 Mainz, Germany
and2 Department of Pathology, Free University Hospital, 1081 HV Amsterdam, The Netherlands
The organization of epitopes on the minor capsid protein L2 of human papillomavirus (HPV) type 33 has been analysed using three monoclonal antibodies (MAbs) generated against a large fragment of the L2 protein (amino acids 82259) expressed as a glutathione S-transferase fusion protein. The topology of the L2 epitopes has been investigated with respect to the structure of HPV-33 virus-like particles (VLPs). Two of the MAbs reacted with linear epitopes which were mapped to amino acids 153160 and 163170, respectively. These epitopes were accessible in denatured but not in native VLPs consisting of L1 and L2, suggesting an internal location. The third antibody was unable to detect denatured L2 protein but reacted with native VLPs. This is the first demonstration of an apparent conformational epitope of the HPV L2 protein. A model for the putative orientation of L2 in the papillomavirus capsid is deduced from the location of these and other antigenic sites.
* Author for correspondence. Fax +49 6131 392 359.
Received 3 May 1995;
accepted 29 June 1995.
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