Interactions between papillomavirus L1 and L2 capsid proteins.
The human papillomavirus (HPV) capsid consists of 360 copies of the major capsidprotein, L1, arranged as 72 pentamers on a T=7 icosahedral lattice, with substoichiometric amounts of the minor capsid protein, L2. In order to understand the arrangement of L2 within the HPV virion, we have defined and biochemically characterized a domain of L2 that interacts with L1 pentamers. We utilized an invivo binding assay involving the coexpression of recombinant HPV type 11 (HPV11)L1 and HPV11 glutathione S-transferase (GST) L2 fusion proteins in Escherichia coli. In this system, L1 forms pentamers