Solutions for RABV vaccine and drug development

Rabies virus (RABV) is a neurotropic virus that causes rabies in humans and animals, occurring in more than 150 countries and territories. Once clinical symptoms appear, rabies is virtually 100% fatal. Despite the availability of post-exposure vaccines, rabies remains a global health threat.

The causative agent of rabies, RABV, is a negative-stranded RNA virus of the genus Lyssavirus. RABV is a member of the Rhabdoviridae family, named for the characteristic rod- or bullet-shaped rhabdovirus virion observed by electron microscopy. Rhabdovirus virions, like other negative-stranded RNA viruses, are composed of a highly stable and organized complex of genomic RNA and nucleoprotein, contained in a lipid envelope derived from the host cell membrane.

Existing vaccines target the rabies virus glycoprotein (RABV-G). However, these vaccines induce short-lived immune responses potentially due to the heterogeneous nature of RABV-G under physiological conditions. Recent research suggests that incorporating trimeric, prefusion RABV-G bound to a potent and broadly neutralizing antibody into vaccine design is crucial for presenting the correct conformation of the protein and eliciting a robust immune response. Nucleic acid-based vaccines offer an alternative approach, potentially bypass purification issues, but must still ensure the expression of glycoproteins with the correct conformation and quaternary assembly.

While RABV-G remains a primary focus for vaccine development, the nucleoprotein (N) has emerged as a promising alternative target. Studies demonstrate that N can induce robust T helper cell responses and long-lasting humoral immunity, making it a valuable candidate for next-generation rabies vaccines.

N plays a central role in RABV replication, encapsidating the viral genome and forming the viral ribonucleoprotein (RNP) complex, which serves as the template for viral transcription and replication. Additionally, the amino acids at positions 273 and 394 in the N protein are important for both evasion of the host RIG-I-mediated antiviral response and pathogenicity.

The development and improvement of vaccines remain the current prevention and control of the principal means of RABV infection. Explore our comprehensive suite of solutions for RABV vaccine development!

SEC-MALS

Purity of RABV Glycoprotein G, His Tag (Cat. No. RAG-V55H5) exceeds 85%, with a verified molecular weight of approximately 165-195 kDa by SEC-MALS analysis.

ELISA

Immobilized RABV Glycoprotein G, His Tag (Cat. No. RAG-V55H5) at 1 μg/mL (100 μL/well) demonstrates a linear binding range of 0.1-2 ng/mL with Mouse Glycoprotein G Antibody, Mouse IgG1 (523-11) (Cat. No. RAG-M305) (QC tested).

Protocol

To assess the precision of RAS-A167, repeat it 20 times to assess the accuracy within the plates and 3 times for three known concentrations to assess the accuracy between the plates. The within and inter-plate precision of the project is CV＜9%, better than the standard range stated by the kit (CV＜15%).

To assess the dilution linearity of RAS-A167, high-value spiked samples were analyzed after gradient dilution. The results showed that the average recovery of all analyzed samples was between 80% and 120%, better than the accepted range.

To assess the matrix effect of RAS-A167, different proportions of media interfered with the standard, which showed that 10% of 1640 media and 10% of DMEM media met the standard (RSD<15%). If 100% medium is used, MRD=10 is recommended.