Rabies Virus Glycoprotein

Rabies virus stands as both the representative member and the leading cause of human rabies within the Lyssavirus genus of the Rhabdoviridae family. The main transmission route for rabies virus occurs through animal bites with dogs being the most common carriers. The virus enters the host body and rapidly multiplies within the central nervous system creating severe neurological damage that leads to up to 100% mortality. Effective rabies vaccines provide partial protection yet approximately 60,000 people die from rabies every year worldwide.

Our Rabies Virus Glycoprotein antigen and antibody products delivers advanced precision and efficiency as a research tool for vaccine development and viral neutralization assays against the backdrop of rabies devastation：

Antibodies

Anti-RABV Glycoprotein polyclonal antibody

Anti-RABV Glycoprotein Monoclonal antibody, Clone 3E7

Anti-RABV Glycoprotein Monoclonal antibody, Clone 2D6

Antigens

Recombinant Rabies virus Glycoprotein (aa 20-458)[His]

Recombinant RABV Glycoprotein [His]

Molecular Mechanisms

In recent years, by adopting a fusion-loop substitution strategy, we have successfully obtained a homogeneous RABV-G ectodomain protein. Crystal structures have been resolved at approximately pH 8.0 (in the free state) and pH 6.5 (in the antibody-bound state), revealing key insights:

• Dual Conformations: Pre-fusion and Post-fusion States

Under alkaline conditions, the glycoprotein ectodomain adopts a bent, hairpin conformation that represents the typical pre-fusion state. In contrast, under acidic conditions, the structure becomes elongated, indicating a post-fusion conformation. These different states not only uncover the essential structural transitions during viral entry but also provide a theoretical basis for the exposure of various antigenic epitopes.

• Trimer Assembly and Epitope Mapping

Although the crystal structures of VSV-G and CHAV-G have been determined, RABV-G displays unique molecular organization. Extensive studies indicate that RABV-G tends to assemble as a homotrimer, with critical regions interplaying among each monomer. This insight lays the foundation for designing specific antibodies and developing polyvalent vaccines.

• Impact of N-Glycosylation on Conformation and Immunogenicity

The presence of multiple essential N-glycosylation sites in RABV-G ensures accurate protein folding and structural stability while also affecting epitope exposure and immune system recognition. Through careful preservation methods during purification we maintain natural glycosylation modifications which enable our product to represent the native state of the virus for molecular dynamics simulations and vaccine design.

Application Prospects

• Vaccine Development

The research community can produce vaccine candidates that target multiple antigenic epitopes which generate broad-spectrum neutralization and immune protection using a fully glycosylated RABV-G ectodomain. Vector-based and in situ immunomodulatory strategies promise to enable the production of low-cost single-dose recombinant vaccines.

• Neutralizing Antibody Screening and Evaluation

This product functions as a reliable benchmark for antibody detection techniques such as ELISA and flow cytometry while maintaining accuracy during molecular dynamics simulations to evaluate vaccine effectiveness and neutralizing antibody responses.

Research examinations focus on understanding viral entry processes alongside receptor binding interactions.

Research into the pH-driven structural changes of RABV-G helps scientists understand viral interactions with host cell receptors. These insights provide essential information for the creation of new antiviral treatments and medical therapies.

Figure 2. Stability analysis of rRABV G protein. (Source: Li Q, et al. 2023)

RABV Glycoprotein Antibodies

RABV Glycoprotein Antigens

Rabies Virus ELISA Kits