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The envelope glycoprotein GP64 of Autographa californica nucleopolyhedrovirus (AcMNPV) is necessary and sufficient for the acid-induced membrane fusion activity that is required for fusion of the budded virus (BV) envelope and the endosome membrane during virus entry. Infectivity of the budded virus (BV) is neutralized by AcV1, a monoclonal antibody (MAb) directed against GP64. Prior studies indicated...
The minor capsid protein L2 of papillomaviruses (PVs) likely plays a role in the selective encapsidation of PV DNA in viral capsids and in the infectivity of PV virions. The L2 protein also can cause the relocalization of the PV early protein, E2TA, to nuclear subdomains known as promyelocytic leukemia oncogenic domains (PODs) in which it is localized. E2TA is a transcriptional transactivator that...
We have previously described a DNA-packaging assay using bovine papillomavirus type 1 (BPV-1) virus-like particles (VLPs) and have identified a region of the BPV genome that assists in packaging. In this study, we identify a specific BPV sequence involved in DNA packaging by BPV-1 VLPs. In the initial screening of BPV-1 genomic sequences essential for DNA packaging, we observed that a plasmid with...
It has been shown previously that recombinant virus-like particles (VLPs) of papillomavirus can induce VLP-specific humoral and cellular immune responses following parenteral administration. To test whether mucosal administration of bovine papillomavirus type 1 (BPV1) VLPs could produce mucosal as well as systemic immune responses to VLPs, 50 μg chimeric BPV1 VLPs containing an HPV16 E7 CTL epitope...
Mouse monoclonal antibodies (mAbs) were raised against the major capsid protein, L1, of human papillomavirus type 16 (HPV16), produced inEscherichia coliwith the expression plasmid pTrcL1. Epitope specificity could be assigned to 11 of these 12 antibodies using a series of linear peptides and fusion proteins from HPV16. One mAb (MC53) recognized a novel linear epitope that appears to be unique to...
Encapsidation of circular DNA by papillomavirus capsid protein was investigated in Cos-1 cells. Plasmids carrying both an SV40 origin of replication (ori) and anE. coli oriwere introduced into Cos-1 cells by DNA transfection. PV capsid proteins were suppliedin transby recombinant vaccinia viruses. Pseudovirions were purified from infected cells and their packaged DNA was extracted and used to transformE...
To evaluate an antigen delivery system in which exogenous antigen can target the major histocompatibility complex (MHC) class I pathway, a single human papillomavirus (HPV) 16 E7 cytotoxic T lymphocyte (CTL) epitope and a single HIV gp160 CTL epitope were separately fused to the C-terminus of bovine papillomavirus 1 (BPV1) L1 sequence to form hybrid BPV1L1 VLPs. Mice immunized with these hybrid VLPs...
We have constructed chimeric papillomavirus-like particles (CVLPs) by replacing the 34-carboxy-terminal amino acids of the HPV 16 L1 protein with various parts of the HPV 16 E7 protein. Chimeric proteins were expressed by recombinant baculoviruses and analyzed by electron microscopy for their ability to assemble into virus capsids. We were able to produce CVLPs in high efficiencies with inserts of...
The bovine papillomavirus type 1 (BPV1) L2 protein purified fromEscherichia coliwas used as an antigen to produce monoclonal antibodies (MAbs). A total of 26 individual clones which recognized the BPV1 L2 protein were obtained. Using infectious BPV1 virus particles, 3 of the MAbs were found to interact with BPV1 virus particles. Binding of the MAbs to BPV1 was confirmed by immunoelectron microscopy...
The papillomavirus major capsid protein L1 can assemble into capsidsin vitro.To identify 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...
We examined the distribution of putative receptors for papillomavirus (PV) capsid proteins on various cell types, using either Hexahis HPV6b L1 fusion protein or synthetic HPV6b virus-like particles (VLPs). Specific, saturable binding of VLPs to CV-1 cells was demonstrated using 35 S-labeled VLPs, with an average receptor number of 1 × 10 4 /cell and a binding affinity constant (K...
The fate of full bovine papillomavirus (BPV) virions and virus-like particles after binding to C127 or CV-1 cells was studied by electron microscopy and indirect immunofluorescence. After incubation at 4° for 1 hr, BPV virions were found to be bound to the plasma membrane, and most viruses were absorbed by the cells after 30 min incubation at 37°. Ninety minutes after the virions had been bound to...
The L2 protein of the human papillomaviruses is a minor structural protein and is not necessary for the major L1 protein to assemble into capsids. However L2 protein binds DNA and enhances the efficiency of HPV capsid assembly, suggesting an important role in the production of infectious papillomaviruses. L2 accumulates rapidly in the nucleus after synthesis in the cytoplasm. To identify L2 sequences...
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