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.

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 ...

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.

2018年7月6日 · Bovine papillomavirus-1 (BPV-1), the aetiological agent of equine sarcoids, primarily causes warts in its natural host, the cattle, it can also cause locally aggressive and invasive skin tumours in horses, known as sarcoids, and thus provides a rare example of inter-species transmission of a papillomavirus (Trewby et al. 2014).

2009年10月10日 · The L1 major capsid proteins of BPV1 and BPV2 were expressed in Sf-9 insect cells and both self-assembled into virus-like particles (VLPs). Using conformation-dependent monoclonal antibodies (mAb) both type-specific and shared epitopes were detected.

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.

2023年3月27日 · Here, we describe the production of BPV1 L1 as VLPs in a baculovirus expression vector system (BEVS) and the purification of these particles by Lentil Lectin-Sepharose 4B as a promising method for the preparation of a prophylactic vaccine applicable in veterinary medicine.

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 …

Hypothesis: BPV-1 L1 VLPs may constitute a safe and highly immunogenic vaccine candidate for protection of horses against BPV-1/-2-induced disease. Methods: Three groups of 4 horses each received 50, 100 or 150 µg of BPV-1 L1 VLPs, respectively, on Days 0, 28 and 168.