MOUSE ANTI-RIFT VALLEY FEVER VIRUS NUCLEOPROTEIN (M976)

Rift Valley Fever nucleoprotein (M976) antibody recognises RVFV N protein and is suitable for use in ELISA.

PRODUCT DETAILS – MOUSE ANTI-RIFT VALLEY FEVER VIRUS NUCLEOPROTEIN (M976)

• Mouse anti Rift Valley Fever Nucleoprotein (M976). Recognises RVFV N protein in ELISA.
• Purified by Ion Exchange. >90% purity by SDS-PAGE.
• Presented in phosphate buffered saline, pH 7.2 with 0.05% sodium azide.

BACKGROUND

RVFV was first characterized in 1931 in the Rift Valley region of Kenya when it caused an outbreak among livestock. The causative agent – Rift Valley Fever Virus, is an enveloped RNA virus that belongs to the genus Phlebovirus, of the Bunyaviridae family. Bunyaviruses all share tripartite genomes that consist of large, medium and small RNA segments. The small, (S) segment is responsible for encoding the Bunyavirus Nucleoprotein, which is responsible for the formation of ribonucleoprotein complexes that are essential in the virus life cycle and genome replication (Mottram et al., 2017).

Ferron et al. produced a crystal structure of RVFV nucleoprotein, which shows a hexameric ring with structural flexibility, suggested to allow various RNA-binding conformations. Within the inner portion of the ring, positive residues are shown to bind RNA, which are conserved across different Phlebovirus species. Xu et al. surmise that RVFV N-subunit vaccines are able to induce a cell-mediated response to protect against RVFV in mice and demonstrate that the nucleoprotein is a key immunogen during host infection.

RVFV is an arbovirus, transmitted to domesticated livestock by Aedes and Culex mosquitoes. Cattle, sheep, goats and camels are particularly susceptible to the virus and serve as amplifying hosts (WHO). RVFV can be found in sub-Saharan Africa, Egypt, Yemen, Saudi-Arabia, Mayotte and Madagascar. The continuing geographical expansion of RVFV is also cause for concern on the European continent, where the virus is an emerging threat. Reports of RVFV outbreaks in the region have raised concerns that the virus may spread to temperate climates by its emerging, competent mosquito vectors.

Infection by RVFV can result in several overlapping symptoms, that range from febrile illnesses to blindness, encephalitis and even lethal hemorrhagic fever. Currently, vaccines against RVFV are only partially attenuated, cost-prohibitive and are only able to induce short-lived immunity. No specific therapeutics are available to cure RVFV infection and preventive efforts to avoid new outbreaks are mostly limited to monitoring vector distribution in threatened regions.

REFERENCES

• Ferron et al. (2011). The Hexamer Structure of the Rift Valley Fever Virus Nucleoprotein Suggests a Mechanism for its Assembly into Ribonucleoprotein Complexes. Pathogens.
• Mottram et al. (2017). Mutational analysis of Rift Valley fever phlebovirus nucleocapsid protein indicates novel conserved, functional amino acids. Neglected Tropical Diseases.
• World health organisation (WHO). Rift Valley fever.
• Xu et al. (2013) The Nucleocapsid Protein of Rift Valley Fever Virus Is a Potent Human CD8 T Cell Antigen and Elicits Memory Responses. PLoS ONE 8(3).