pre-F & Glycoprotein G: Advanced Tools for Nipah Vaccine Potency
NiV&HeV: A New Era of Structure-based Vaccine Design?
Nipah virus (NiV) and Hendra virus (HeV) are highly pathogenic bat-borne paramyxoviruses included in the WHO Blueprint priority diseases list. Both are classified biological safety level 4 (BSL-4) viruses listed in Category C biothreat agents by the NIH and CDC. Currently, there are no approved human prophylaxis or therapeutic for NiV or HeV disease.
NiV has two membrane-anchored glycoproteins, the attachment protein (G) and fusion (F) protein, that mediate receptor binding and entry into host cells. G binding to the cellular receptor, ephrin-B2 or -B3, triggers a conformational change in F that facilitates fusion of the viral and cellular membranes. Both the F and G/RBP proteins thus present attractive targets for vaccine design. Similar to respiratory syncytial virus (RSV), immunizing mice with pre-fusion F protein elicits higher titers of neutralizing antibodies compared to post-fusion F.
To support the development of NiV and HeV vaccines, ACROBiosystems has developed high-quality antigens, including:
- Stable trimeric pre-fusion F protein
- Post-fusion F protein
- Glycoprotein G
These antigens have been validated for their high homogeneity using SEC-MALS and their high activity was further confirmed through ELISA or SPR assays. These antigens are ideal for creating ELISA methodologies to evaluating NiV and HeV vaccine candidates. In addition, ACROBiosystems offers a Monoclonal Anti-Nipah Post Fusion Glycoprotein Antibody as a control, enabling precise immunogenicity assessments in vaccine development.
By utilizing ACROBiosystems’ advanced reagents, researchers can achieve optimal results in vaccine development with antigens in their correct native structure. Discover more about the critical role of Pre-F antigens in assessing vaccine efficacy against NiV and HeV on our News page.
