Batch dependent - please inquire should you have specific requirements
Buffer
DPBS, pH 7.4
Preservative
None
Storage
Store at -80°C. Avoid multiple freeze/thaw cycles
Introduction
Nipah virus (NiV) is a member of the family Paramyxoviridae, genus Henipavirus. NiV was initially isolated and identified in 1999 during an outbreak of encephalitis and respiratory illness among pig farmers and people with close contact with pigs in Malaysia and Singapore. Nipah virus is in the newly created Henipavirus genus with the closely related Hendra virus and Cedar virus. The Henipavirus family is pleomorphic, meaning their shape is varied, and traditionally 40 to 600 nm in diameter. The core of a virion contains a linear ribonucleprotein (RNP) comprising of negative sense single stranded RNA.
Antigen Description
Recombinant Nipah Virus Glycoprotein G is produced by HEK293 cells and the target gene encoding a.a 71- 602 is expressed with a Fc tag at the C-terminus.
Keywords
Nipah Virus G Protein; Nipah Virus; G Protein; NiV; NiV G Protein
Citations
Publication ()
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Background
Nipah virus (NiV) is a highly lethal zoonotic paramyxovirus that causes severe respiratory infections and encephalitis. NiV is a negative-sense single-stranded RNA enveloped virus with a non-segmented genome encoding six structural proteins, namely nucleoprotein (N), phosphoprotein (P), matrix protein (M), fusion glycoprotein (F), attachment glycoprotein (G) and RNA polymerase or large protein (L). In addition, as a result of mRNA editing and substitution of start codons, there are three accessory proteins within P: Protein V, Protein W, and Protein C. Based on genome sequence analysis, NiV can be divided into two major clades: the M genotype, which includes Malaysian NiV isolates (NiV-M), and the B genotype, which includes Bangladeshi (NiV-B) and Indian NiV isolates (NiV-I). B clade infections are significantly more pathogenic than M clades.
Figure 1. Schematic representation of the structure of an NiV particle and the viral genome organization (Source: Liew YJM, et al. 2022)
The NiV replication cycle begins when the virus attaches to the host cell receptors ephrin-B2 and ephrin-B3 via the NiV G protein. Unlike other paramyxoviruses, the NiV G protein is unique in that it does not function as a hemagglutinin or neuraminidase. As a type II membrane protein, G proteins exhibit characteristic tetramerization through their N-terminal α-helical stalk domain, while their C-terminal globular head domain binds to host cell receptors. NiV F proteins mediate the fusion of the viral envelope with the host cell membrane, releasing the viral genome into the cytoplasm. Viral genomic RNA is associated with N, P, and L proteins to form ribonucleoprotein complexes that participate in viral transcription and replication. L polymerase catalyzes the transcription of viral genomic RNA into mRNA for protein translation. The translated viral surface glycoproteins F and G are inserted into the host cell endoplasmic reticulum for post-translational modifications such as glycosylation.
NiV infection is commonly associated with acute respiratory distress, encephalitis and in some cases myocarditis, with some patients experiencing lethargy, confusion and even coma. A subset of patients develops residual neurologic complications, such as delayed encephalitis, several years after the initial infection.
Alternative Names
NiV G Protein NiV G
References
1. Liew YJM, et al. The Immunobiology of Nipah Virus. Microorganisms. 2022 Jun 6;10(6):1162.
2. Soman Pillai V, et al. Nipah Virus: Past Outbreaks and Future Containment. Viruses. 2020 Apr 20;12(4):465.
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Figure 1. Schematic representation of the structure of an NiV particle and the viral genome organization
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