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Batai virus
Batai virus (BATV) is a RNA virus belonging to the genus Orthobunyavirus.
Batai virus (BATV) is an enveloped, single-stranded, negative sense RNA genome. It is a member of the genus Orthobunyavirus. It was first isolated from Culex mosquitoes in Malaysia in 1955. Evidence from serological surveillance and virus isolation shows that this virus is widely distributed around the world. Similar to other orthobunyaviruses it contributes to both human and animal disease. In humans it has been noted in causing severe fever, and in bovines has been associated with premature birth, birth defects, and increased abortion rates. It is transmitted through mosquito bites, ticks, and biting midges, and occurs from cold to tropical regions of Africa, Asia, and Europe.
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 S segment encodes the nucleocapsid (N) and the non-structural (NSs) proteins. The M segment encodes the virion surface glycoproteins (Gn, Gc) and non-structural proteins (NSm). The L segment encodes for the replicase/ transcriptase L protein. The nonstructural proteins NSm participate in virus assembly and NSs plays a key role in counteracting the host immune response by blocking alpha/beta interferon induction The full-length genome of NM/12 consists of a 947 base pair nucleotide S segment, a 4405 base pair nucleotide M segment, and a 6870 base pair nucleotide L segment. It also contains one open reading frame that encode three proteins of 151, 943, or 1395 amino acids.
Viral enveloped nucleocapsids utilize membrane glycoproteins on their surface to mediate entry into host cells. Averaging of glycoprotein spikes of membrane viruses, such as HIV-1, has been a particularly successful approach for studying their structure. An understanding of the structure is integral for revealing both the molecular basis of virus–host interactions and guiding antiviral and vaccine design development. A software named Jsubtomo enables visualization of the structure of viral glycoprotein spikes to a resolution in the range of 20-40 Å and allows for study of the study of higher order spike-to-spike interactions on the virion membrane.
Extensive research has yet to be performed on the detailed crystalline structure of Batai virus, but research on the closely related Bunyamwera virus has shown a distinct functionality of each of the two nucleocapsid side chains. 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. Cryo-electron microscopy has also determined that whilst Bunyamwera virions are pleomorphic in shape, they display a locally ordered lattice of glycoprotein spikes. Each spike protrudes 18 nanometers from the viral membrane and becomes disordered upon introduction to an acidic environment.
Although the exact icosahedral symmetry of a Batai virus viron is yet to be determined, studies using Cryo-electron tomography on related viruses of the Bunyaviridae family have shown that there exists an icosahedral lattice with clear T=12 quasisymmetry. Consequently, this triangulation number would correlate with a viral nuclear capsid exhibiting 720 faces. This study was performed on the Rift Valley Fever Virus (RVFV), which is an arthropod borne disease that is endemic to regions of Africa and Asia, namely the Rift Valley in Kenya from which its name is derived.
Batai virus is a member of the genus Orthobunyavirus and a member of the family Bunyaviridae. Batai virus is part of a diverse group of arthropod-borne viruses. Classified via the Baltimore scheme, Batai virus is a negative-sense, single-stranded RNA virus. The orthobunyavirus genome has a characteristic segmented genome, with small, medium, and large (S, M, and L) segments which generally encode the nucleocapsid, envelope protein and the polymerase protein, respectively. The size of the S segment is 943 nucleotides, the size of the M segment is 4440 nucleotides, and the size of the L segment is 6870 nucleotides. In the S segment there are two open reading frames (ORFs), the nucleocapsid and non-structurals which were overlapping. The M segment has a polyprotein precursor in the open reading frame. The L segment encodes for an RNA-dependent RNA polymerase.
Batai virus is geographically spread throughout Asia and Europe. It has been shown that batai viruses from Japan, Malaysia and India share homologies in the genomic sequence more so than when virus strains from Europe and Asia are compared to each other. Reassortment of the genome can have some serious effects. It has been observed that reassortment between the M segment and the S and L segments with another strain of Batai virus (BUNV) can cause an increase in the virulence of Batai virus. Reassortment of the genome within the genus Orthobunyavirus are not uncommon and can lead to an increase in virulence.
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Batai virus
Batai virus (BATV) is a RNA virus belonging to the genus Orthobunyavirus.
Batai virus (BATV) is an enveloped, single-stranded, negative sense RNA genome. It is a member of the genus Orthobunyavirus. It was first isolated from Culex mosquitoes in Malaysia in 1955. Evidence from serological surveillance and virus isolation shows that this virus is widely distributed around the world. Similar to other orthobunyaviruses it contributes to both human and animal disease. In humans it has been noted in causing severe fever, and in bovines has been associated with premature birth, birth defects, and increased abortion rates. It is transmitted through mosquito bites, ticks, and biting midges, and occurs from cold to tropical regions of Africa, Asia, and Europe.
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 S segment encodes the nucleocapsid (N) and the non-structural (NSs) proteins. The M segment encodes the virion surface glycoproteins (Gn, Gc) and non-structural proteins (NSm). The L segment encodes for the replicase/ transcriptase L protein. The nonstructural proteins NSm participate in virus assembly and NSs plays a key role in counteracting the host immune response by blocking alpha/beta interferon induction The full-length genome of NM/12 consists of a 947 base pair nucleotide S segment, a 4405 base pair nucleotide M segment, and a 6870 base pair nucleotide L segment. It also contains one open reading frame that encode three proteins of 151, 943, or 1395 amino acids.
Viral enveloped nucleocapsids utilize membrane glycoproteins on their surface to mediate entry into host cells. Averaging of glycoprotein spikes of membrane viruses, such as HIV-1, has been a particularly successful approach for studying their structure. An understanding of the structure is integral for revealing both the molecular basis of virus–host interactions and guiding antiviral and vaccine design development. A software named Jsubtomo enables visualization of the structure of viral glycoprotein spikes to a resolution in the range of 20-40 Å and allows for study of the study of higher order spike-to-spike interactions on the virion membrane.
Extensive research has yet to be performed on the detailed crystalline structure of Batai virus, but research on the closely related Bunyamwera virus has shown a distinct functionality of each of the two nucleocapsid side chains. 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. Cryo-electron microscopy has also determined that whilst Bunyamwera virions are pleomorphic in shape, they display a locally ordered lattice of glycoprotein spikes. Each spike protrudes 18 nanometers from the viral membrane and becomes disordered upon introduction to an acidic environment.
Although the exact icosahedral symmetry of a Batai virus viron is yet to be determined, studies using Cryo-electron tomography on related viruses of the Bunyaviridae family have shown that there exists an icosahedral lattice with clear T=12 quasisymmetry. Consequently, this triangulation number would correlate with a viral nuclear capsid exhibiting 720 faces. This study was performed on the Rift Valley Fever Virus (RVFV), which is an arthropod borne disease that is endemic to regions of Africa and Asia, namely the Rift Valley in Kenya from which its name is derived.
Batai virus is a member of the genus Orthobunyavirus and a member of the family Bunyaviridae. Batai virus is part of a diverse group of arthropod-borne viruses. Classified via the Baltimore scheme, Batai virus is a negative-sense, single-stranded RNA virus. The orthobunyavirus genome has a characteristic segmented genome, with small, medium, and large (S, M, and L) segments which generally encode the nucleocapsid, envelope protein and the polymerase protein, respectively. The size of the S segment is 943 nucleotides, the size of the M segment is 4440 nucleotides, and the size of the L segment is 6870 nucleotides. In the S segment there are two open reading frames (ORFs), the nucleocapsid and non-structurals which were overlapping. The M segment has a polyprotein precursor in the open reading frame. The L segment encodes for an RNA-dependent RNA polymerase.
Batai virus is geographically spread throughout Asia and Europe. It has been shown that batai viruses from Japan, Malaysia and India share homologies in the genomic sequence more so than when virus strains from Europe and Asia are compared to each other. Reassortment of the genome can have some serious effects. It has been observed that reassortment between the M segment and the S and L segments with another strain of Batai virus (BUNV) can cause an increase in the virulence of Batai virus. Reassortment of the genome within the genus Orthobunyavirus are not uncommon and can lead to an increase in virulence.