Interactions between papillomavirus L1 and L2 capsid proteins.
Journal Article
Overview
abstract
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