[2] The structure of Batai virus (BATV) consists of an enveloped nucleocapsid that is composed of three RNA segments: small (S), medium (M), and large (L).

The M segment encodes the virion surface glycoproteins (Gn, Gc) and non-structural proteins (NSm).

[2] Viral enveloped nucleocapsids utilize membrane glycoproteins on their surface to mediate entry into host cells.

[4] An understanding of the structure is integral for revealing both the molecular basis of virus–host interactions and guiding antiviral and vaccine design development.

An N-terminal arm and a C-terminal tail were found to interact with neighboring NP protomers to form a tetrameric ring-shaped organization.

Each protomer bound a 10-nucleotide RNA molecule, which was acquired from the expression host, in the positively charged crevice between the N and C lobes.

[5] Cryo-electron microscopy has also determined that whilst Bunyamwera virions are pleomorphic in shape, they display a locally ordered lattice of glycoprotein spikes.

The most common vertebrate affected by BATV are domestic pigs, horses, ruminants and wild birds, which have been known to be the primary mammalian hosts.

[10] At the onset of replication the virus particles coalesce into vacuole membranes lining the cytoplasm of the infected cells.

Encoded by the M RNA segment they are involved in attachment to the host cell through unidentified receptors on the surface and elicit neutralizing antibodies.

These newly assembled viral particles will mature over a period of time inside of the hosts cell in the membranes of the Golgi apparatus before being released.

This stems from the viruses ability to form clear lytic plaques in cells of vertebrate species but not in those derived from insects.

[13] Similar NSs proteins of the Rift Valley fever phlebovirus have quite a distinct size and amino acid sequence, but they play a similar role in mammalian cells in overcoming the innate immune responses that are a consequence of the global shut-down of the cells transcription mechanisms.

Similar NSs proteins of the Rift Valley fever phlebovirus have quite a distinct size and amino acid sequence, but they play a similar role in mammalian cells in overcoming the innate immune responses that are a consequence of the global shut-down of the cells transcription mechanisms.

Infection results in high fever, chills, severe headache, dizziness, back, and abdominal pains.