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Solutions for RABV vaccine and drug development

Rabies Virus (RABV)
Rabies virus structure
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. According to the 2018 International Committee on Taxonomy of Viruses (ICTV), 16 species of the genus Lyssavirus are classified into 3 different genetic phylogroups (Phylogroup I-III). Rabies virus (RABV), which is currently prevalent in China, belongs to genetic phylogroup I.
Rabies Vaccine Market Status
Currently, human rabies vaccines approved for marketing in China can be divided into 3 categories based on different culture substrates: Vero cell purified vaccine, human diploid cell vaccine, and hamster kidney primary cell purified vaccine. Currently, Vero cell-cultured rabies vaccines are mainstream, human diploid rabies vaccines are developing and gradually gaining market share, and new gene engineering vaccines (mRNA rabies vaccines) are also making breakthrough progress.
Key Targets for Rabies Vaccine Design
RABV mainly has nucleoprotein N and glycoprotein G as two antigens. Nucleoprotein N cannot produce protective antibodies after stimulating the body, but can participate in specific antigen recognition and immune memory.
Rabies virus glycoprotein G is the only exposed protein on the virus surface and is also the target of neutralizing antibodies induced by vaccines.
Rabies virus G protein is structurally heterogeneous. The sequence of rabies virus glycoprotein can unfold and flip upward when needed. It can switch conformations during the process before and after fusion with host cells, such as: from trimer structure to monomer structure. Human antibodies recognize a single site on the protein. But when a protein is hidden or this site is moved, antibodies will not be able to recognize it, resulting in poor longevity of immune responses after vaccination. Most rabies vaccines are made from inactivated viruses. During virus inactivation, the G protein will be deformed, and the vaccine cannot show the immune system the "full appearance" of the virus. Therefore, the correct conformation of glycoprotein is extremely important for guiding improved vaccine design and determining therapeutic targets.
The research team led by the La Jolla Institute for Immunology in the United States and the Pasteur Institute in France captured the high-resolution three-dimensional structure of rabies virus glycoprotein G trimer bound to "prefusion" specific neutralizing antibodies, confirming that the glycoprotein trimer interface involves interactions between central α-helices and adjacent loops, as well as the role of fusion loops in trimerization and prefusion conformation stabilization, providing design pathways for developing more effective vaccines.

RABV vaccines and drugs R&D development solutions

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!

Mouse Anti-RABV Nucleoprotein Antibody IgG Titer Serologic Assay Kit (ELISA) are available!NEW

Native, structurally verified trimeric glycoprotein (G) & RABV-G specific antibodies.

RABV Nucleoprotein (N) verified through ELISA with specific antibodies.

High quality RABV-G Antigen/antibody ELISA kits

Product List

Kits
Antigen
Antibody

Assay Data

trimeric glycoprotein (G) (Cat. No. RAG-V55H5)
SEC-MALS
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
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).

Rabies virus Glycoprotein G ELISA Kit (Cat. No. RAS-A167)
High Precision

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%).

High Precision
Dilution linearity is better than the standard

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.

Dilution linearity is better than the standard
Matrix effect met the criteria

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.

Matrix effect met the criteria

Resources

Core Reagents for Infectious Disease Research
  • Background
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