CONFORMATIONAL AND LINEAR EPITOPES ON VIRUS-LIKE PARTICLES OF HUMAN PAPILLOMAVIRUS TYPE-33 IDENTIFIED BY MONOCLONAL-ANTIBODIES TO THE MINORCAPSID PROTEIN L2

.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 82-259) expressed as a glutathione S-transferase fusion protein. The topology of the L2 epitopes has been investigated with re spect to the structure of HPV-33 virus-like particles (VLPs). Two of t he MAbs reacted with linear epitopes which were mapped to amino acids 153-160 and 163-170, respectively. These epitopes were accessible in d enatured 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 demonstrati on of an apparent conformational epitope of the HPV L2 protein. A mode l for the putative orientation of L2 in the papillomavirus capsid is d educed from the location of these and other antigenic sites.