Carboxyl terminus of bovine papillomavirus type-1 L1 protein is not required for capsid formation

Abstract

The papillomavirus major capsid protein L1 can assemble into capsids in vitro. To identity areas within the bovine papillomavirus type-1 L1 (BPV L1) protein that are important for virus assembly, we constructed a set of 24 baculovirus recombinants expressing BPV L1 deletion mutants that span the entire L1 open reading frame. Virus-like particle (VLP) formation of the L1 mutants was examined by electron microscopy. Wild-type (wt) BPV L1 expressed in recombinant baculovirus formed VLPs, while capsomeres and aggregates were seen for most of the mutants screened. However, the C-terminal truncation mutant, lacking the last 24 amino acids (ΔC2), was observed to form VLPs (threefold more efficiently than wt BPV L1). This suggests that this C-terminal region of L1 protein is not critical for capsid formation. As capsids assembled from BPV L1 are able to agglutinate mouse red blood cells (RBC) by binding to a membrane protein, we tested the ability of the mutants to hemagglutinate mouse RBCs. Most aberrant capsids or aggregates derived from deletion mutants were unable to agglutinate the RBCs with the exception of deletion mutants Δ11 (aa 231-271), Δ14 (aa 291-331), Δ21 (aa 431-471), and the carboxyl-terminus truncation mutant ΔC2.