Applications: WB Reactive species: Nipah Virus
"Abstract: Nipah virus (NiV) and Hendra virus (HeV) are classified as high-consequence zoonotic viruses characterized by high pathogenicity and high mortality in animals and humans. Rapid diagnosis is essential to containing the outbreak. In this study, the henipavirus receptor ephrin B2 was examined to determine whether it could be used as a universal ligand for henipavirus detection in immunoassays. Enzyme-linked immunosorbent assays (ELISAs) were developed using recombinant ephrin B2 as the capture ligand and two monoclonal antibodies (mAbs) as detection reagents. Using mAb F27NiV-34, which cross-reacts with NiV and HeV, we were able to detect NiV and HeV, while mAb F20NiV-65 was used to detect NiV. Therefore, using these two ELISAs, we were able to differentiate between NiV and HeV. Furthermore, we developed a rapid lateral flow strip test for NiV detection using ephrin B2 as the capture ligand combined with mAb F20NiV-65 as the detector. Taken together, our results show that the combination of ephrin B2 and a specific mAb provides an excellent pairing for NiV and HeV detection." Article snippet: Microtitre plates (*) were coated with rabbit poly anti-NiV-G (1:2K, Creative Diagnostics, USA) or recombinant ephrin B2, or B3 (25 ng/well, *) in a carbonate/bicarbonate buffer at a pH 9.6 overnight at 4 ℃.
Figure 1. Comparison of ephrin B2 and polyclonal NiV-G for capture of Henipavirus in sandwich ELISA
Applications: WB Reactive species: NiV
"Abstract: Nipah virus (NiV), a highly lethal zoonotic paramyxovirus, displays strain-specific pathogenicity, yet the molecular basis for this divergence remains elusive. Here, we identify N6-methyladenosine (m6A) modification as a pivotal regulator of NiV replication. Higher m6A methylation levels on viral genomic RNA and mRNAs are associated with the increased virulence observed in the NiV-Malaysia (NiV-M) strain compared to NiV-Bangladesh (NiV-B). Underlying this phenomenon, NiV infection orchestrates a reprogramming of the host m6A machinery by downregulating the methyltransferase METTL3 and the demethylase ALKBH5, while concurrently upregulating m6A reader proteins YTHDF1-3. Both METTL3 and ALKBH5 bind directly to NiV RNA, with METTL3 installing m6A to promote viral replication and ALKBH5 removing them to inhibit it. Strikingly, pharmacological inhibition of m6A modification markedly attenuates NiV replication in vitro and in vivo, underscoring the therapeutic potential of targeting the m6A pathway. Our study establishes m6A as a key determinant of NiV pathogenicity and provides a paradigm for host-directed antiviral strategies against high-risk RNA viruses." Article snippet: The primary antibodies used in this study included mouse monoclonal antibodies against***; rabbit polyclonal antibody against NiV G (CABT-L11VR, CD Creative Diagnostics, Shirley, NY, USA), ***.
Figure 1. Western blot of m6A-related proteins after overexpression of NiV N, P, G, or L.
Background
NiV is a highly pathogenic paramyxovirus that emerged in the late 1990s and causes severe respiratory and neurological diseases in humans. The glycoproteins of NiV, namely the receptor-binding G protein and the fusion protein F, are crucial for the virus to attach to and enter host cells. The G protein of NiV is a type II membrane glycoprotein that primarily functions as a receptor-binding protein. Unlike many other paramyxoviruses, the NiV G protein lacks hemagglutinating and neuraminidase activities and does not bind to carbohydrate moieties. Recent studies have identified ephrin B2 as the cellular receptor for NiV, with ephrin B3 being proposed as an alternative receptor. The distribution of ephrin B2 in various cell types and tissues helps explain the cell tropism and broad host range of NiV. The fusion protein F of NiV is another critical glycoprotein involved in the fusion of viral and cellular membranes during virus entry and cell-to-cell fusion. The precursor protein F0 is inactive and needs to be cleaved into F1 and F2 subunits to become fusion-active. The cleavage releases the fusion peptide at the N terminus of F1, allowing it to promote membrane fusion. The proteolytic processing of NiV F protein occurs at the cell surface following endocytosis and is facilitated by the acidic environment of endosomes.
Figure 1. NiV viral infection in the host cell through the binding of G protein and Ephrin B2. (Source: Lin, H., 2023)
Studying the NiV glycoproteins is crucial for understanding the mechanisms of viral entry, tropism, and pathogenesis. Anti-Nipah virus (NiV) Glycoprotein polyclonal antibody is an important tool in the field of virology and immunology for detecting and studying the glycoproteins of the Nipah virus. Anti-NiV Glycoprotein polyclonal antibody can be used in various scientific applications, including Western blotting, enzyme-linked immunosorbent assays (ELISA), immunofluorescence, and immunohistochemistry. By specifically binding to the NiV glycoproteins, the antibody allows researchers to detect and quantify the presence of NiV in samples, study the expression and localization of the glycoproteins in infected cells or tissues, and investigate the immune response against NiV infection. Moreover, the Anti-NiV Glycoprotein polyclonal antibody can aid in deciphering the mechanisms of NiV infection, viral tropism, host immune responses, and the development of potential therapeutic interventions and vaccines.
Alternative Names
Rabbit Anti-Nipah virus (NiV) Glycoprotein polyclonal antibody Anti-Nipah virus (NiV) G protein polyclonal antibody Anti-Nipah virus (NiV) G glycoprotein polyclonal antibody Anti-NiV Glycoprotein polyclonal antibody Anti-NiV G protein polyclonal antibody Anti-NiV G glycoprotein polyclonal antibody
References
1. Lin H. Nipah Virus: A Zoonotic Virus Transmitted from Bats and Pigs, Causing an Epidemic in Southeast Asia. Advances in Infectious Diseases. 2023, 13(2): 283-290.
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References
An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections
Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness with fatality rates of 50–100%. No vaccines or licensed therapeutics currently exist to protect humans against NiV or HeV. HNVs enter host cells by fusing the viral and cellular membranes via the concerted action of the attachment (G) and fusion (F) glycoproteins, the main targets of the humoral immune response. Here, we describe the isolation and humanization of a potent monoclonal antibody cross-neutralizing NiV and HeV. Cryo-electron microscopy, triggering and fusion studies show the antibody binds to a prefusion-specific quaternary epitope, conserved in NiV F and HeV F glycoproteins, and prevents membrane fusion and viral entry. This work supports the importance of the HNV prefusion F conformation for eliciting a robust immune response and paves the way for using this antibody for prophylaxis and post-exposure therapy with NiV- and HeV-infected individuals.
Hendra virus (HeV) and Nipah virus (NiV) are henipaviruses (HNVs) causing respiratory illness and severe encephalitis in humans, with fatality rates of 50–100%. There are no licensed therapeutics or vaccines to protect humans. HeV and NiV use a receptor-binding glycoprotein (G) and a fusion glycoprotein (F) to enter host cells. HNV F and G are the main targets of the humoral immune response, and the presence of neutralizing antibodies is a correlate of protection against NiV and HeV in experimentally infected animals. We describe here two cross-reactive F-specific antibodies, 1F5 and 12B2, that neutralize NiV and HeV through inhibition of membrane fusion. Cryo-electron microscopy structures reveal that 1F5 and 12B2 recognize distinct prefusion-specific, conserved quaternary epitopes and lock F in its prefusion conformation. We provide proof-of-concept for using antibody cocktails for neutralizing NiV and HeV and define a roadmap for developing effective countermeasures against these highly pathogenic viruses.
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Figure 1. Comparison of ephrin B2 and polyclonal NiV-G for capture of Henipavirus in sandwich ELISA 
Figure 1. Western blot of m6A-related proteins after overexpression of NiV N, P, G, or L. 
Figure 1. NiV viral infection in the host cell through the binding of G protein and Ephrin B2.
