There is no product in the shopping cart, buy it!
Rabies virus (RABV), a member of the Lyssavirus genus in the Rhabdoviridae family, possesses a negative-sense RNA genome encoding five structural proteins: nucleoprotein (N), phosphoprotein (P), matrix protein (M), glycoprotein (G), and viral RNA polymerase (L). The G protein is the only transmembrane protein on the surface of the rabies virus and plays a crucial role in viral attachment and infection through interactions with specific cell surface receptors. Moreover, the G protein is the primary antigen responsible for initiating the production of virus-neutralizing antibodies, making it a central target in vaccine development against rabies. The G protein features three potential N-linked glycosylation sites at Asn37, Asn247, and Asn319 in its extracellular domain. These glycosylation sites are vital for ensuring the correct expression and functionality of the G protein. Changes in the number of N-glycosylation sites and the efficiency of glycosylation at specific sites of the G protein can affect virus properties, such as infectivity, pathogenicity, and immunogenicity. A thorough understanding of these glycosylation patterns is essential for comprehending viral infection dynamics and circulation, with implications for vaccine development and public health strategies.
Fig.1 3D structure of rabies virus.1
Since the G protein plays a key role in eliciting neutralizing antibodies, it holds significant potential for the development of a safe and effective subunit vaccine. Creative Biolabs offers comprehensive glycosylation analysis services for RABV G protein across different RABV variants, allowing for an in-depth exploration of the role of site-specific N-glycosylation in viral infection and evolution. Leveraging a combination of cutting-edge glycomic and glycoproteomic approaches, such as lectin microarray and tandem mass spectrometry technologies, we provide detailed information on glycosylation sites and glycosylation patterns at particular sites. Our glycosylation analysis services provide valuable insights into the impacts of N-liked glycosylation of the G protein on viral infectivity, pathogenicity, and evolution of RABV.
Creative Biolabs has amassed extensive expertise in glycosylation analysis of viral glycoproteins. Our glycosylation analysis services for RABV G protein offer valuable insights into the intricate relationship between site-specific N-glycosylation and viral virulence and evolution. If you seek detailed information or have specific inquiries related to research on rabies virus glycoprotein, please feel free to contact us.
Reference