2017年3月14日 · Moreover, the absence of papillomavirus replication in vitro makes the use of recombinant protein a promising candidate for vaccine formulations. Hence, we developed an integrated study on the L1 capsid protein of BPV-1, obtained from a bacterial expression system, regarding its purification, biosafety, thermostability and immunogenicity.

2023年6月7日 · We developed a platform technology by genetically engineering the bovine papillomavirus L1 major capsid protein to insert a polyglutamic acid/cysteine motif in place of wild-type amino acids in the HI loop. Virus-like particles (VLPs) are formed by self-assembly in insect cells infected with a recombinant baculovirus.

Bovine papillomavirus VLPs are 50 nm particles composed of 360 molecules of L1 proteins that form capsomeres of 5 L1 proteins and capsids of 72 capsomeres. The L1 protein was engineered to contain 8 glutamic acids and a cysteine replacing 9 native amino acids at the tip of a surfaced exposed loop, designated the HI loop.

Here, we utilized a mucosal vaccine vector, bovine papillomavirus (BPV) virus-like particles (VLPs), as a platform to present HIV-1 neutralizing epitopes by inserting the extended 2F5 or 4E10 epitope or the MPER domain into D-E loop of BPV L1 respectively.

2017年3月14日 · In this preliminary study, we aimed to integrate data about BPV-1 L1 gene cloning and expression from a bacterial system (E. coli). Afterward, we characterized the L1 recombinant protein and structure of VLPs regarding their biosafety and thermostability. Additionally, we evaluated the potential of L1 to serve as a prophylactic immunogenic ...

1998年4月10日 · BPV-1 L1+L2 VLPs packaged a plasmid containing BPV-1 sequence 8.2 ± 3.1 times more effectively than a plasmid without BPV sequences.

BPV protein L1 gene transfection in the Drosophila melanogaster S2 cell expression system failed to produce L1 protein notwithstanding correct L1 gene insertion. ... The development of a bovine papillomavirus (BPV) vaccine is an outstanding challenge.

L2 possesses a second independent L1 interaction domain located between residues 129 and 246. This interaction was detected in vivo, but not in vitro. Both L1 interaction domains are necessary for L2 to efficiently encapsidate the BPV1 genome in BPHE-1 cells.

1996年9月1日 · The papillomavirus major capsid protein L1 can assemble into capsids in 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 ent …

Immunodominant, conserved and type-restricted external epitopes of bovine papillomavirus (BPV) major (L1) capsid protein have been identified using BPV particles and synthetic peptides. Antisera to disrupted BPV-1 recognized BPV-1 and BPV-2 particles in immune electron microscopy (IEM) studies and i …