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Unveiling the WHO-Prioritized Nipah Virus: Deadly Bat-Borne Pathogen Uncovered

Release date: 2025-08-14 View count: 26

From May to July 2025, Kerala, India, reported four confirmed cases of Nipah virus (NiV), with two fatalities. This marks the ninth NiV outbreak in the state since 2018 and the first confirmed cases in the Palakkad district. The World Health Organization (WHO) identifies Nipah virus as a highly lethal bat-borne virus that can spread through contact with infected animals (particularly fruit bats and pigs), contaminated food, or close contact with infected individuals. No approved vaccines or specific treatments are currently available, with a case fatality rate ranging from 40% to 100%.

Figure 1. Global Distribution of Nipah Virus (NiV) Outbreaks

Viral Structure

The Nipah virus belongs to the Paramyxoviridae family, genus Henipavirus, alongside Hendra virus (HeV). It is a negative-sense single-stranded RNA virus with a genome approximately 18.2 kb in length, encoding six structural proteins and three non-structural proteins. Its natural hosts are fruit bats of the Pteropus genus, prevalent in South and Southeast Asia. In humans, NiV can cause severe respiratory infections and acute encephalitis.

Nipah Virus Structure and Proteins

Figure 2. Nipah Virus Structure and Proteins

Viral Protein Functions

Protein Full Name Primary Function
N Nucleocapsid protein Encapsulates RNA, forming the nucleocapsid complex, protecting the genome, and aiding in replication and transcription
P Phosphoprotein Polymerase cofactor, stabilizes the L protein, and generates V/W proteins through RNA editing
M Matrix protein Links the nucleocapsid to envelope glycoproteins, facilitating virus assembly and budding
F Fusion protein Mediates fusion of the viral envelope with the host membrane, requiring protease cleavage for activation
G Glycoprotein Binds to host receptors Ephrin-B2/B3, determining host range and tropism
L Large polymerase Core enzyme responsible for mRNA synthesis and genome replication

Pathogenesis

The pathogenicity of the Nipah virus primarily relies on glycoprotein-mediated receptor binding and immune evasion. The viral G protein recognizes and binds to the host cell receptors Ephrin-B2/B3, triggering a conformational change in the F protein to mediate membrane fusion, releasing the RNA genome encapsulated by the N protein into the cell. Once inside, the P protein and its derivatives (C, W, V proteins) inhibit innate immune responses by blocking interferon signaling pathways, such as JAK-STAT, creating favorable conditions for efficient viral replication and spread within the host. Additionally, the F protein induces fusion between infected and neighboring cells, forming multinucleated giant cells that enable direct cell-to-cell transmission, further evading immune clearance. In the central nervous system, the virus can cross the blood-brain barrier to infect neurons, causing encephalitis. In the respiratory system, it targets lung endothelial and parenchymal cells, leading to acute respiratory dysfunction.

Nipah Virus Pathogenesis

Figure 3. Nipah Virus Pathogenesis

Epidemiology and Outbreak History

Since its first outbreak in Malaysia in 1998, Nipah virus has caused near-annual winter outbreaks in Bangladesh and multiple outbreaks in India, including in West Bengal (2001, 2007) and Kerala (2018, 2023, 2024). The average case fatality rate is approximately 70%, with some outbreaks reaching 91%. The WHO has designated NiV as a priority high-fatality pathogen for research.

Research Progress

January 2024: The University of Oxford initiated the first human trial for the ChAdOx1 NipahB vaccine, evaluating its safety and immunogenicity.

August 2024: Phylex Biosciences in the U.S. developed an mRNA nanoparticle vaccine that induced strong neutralizing antibody responses in mice with a single dose.

August 31, 2024: Deng Zengqin's team at the Wuhan Institute of Virology, China, developed a G protein head domain nanoparticle vaccine capable of neutralizing three pathogenic henipaviruses.

July 8, 2025: The University of Queensland, Australia, developed a bispecific antibody, D590-m102.4, which provided 100% protection in hamsters when used prophylactically.

July 10, 2025: The U.S. PHV02 vaccine is preparing for Phase II clinical trials, with Phase I demonstrating safety and immunogenicity. No specific antiviral drugs or vaccines are currently approved. Diagnosis relies primarily on RT-PCR and ELISA to detect NiV nucleic acids or specific antibodies.

Key Research Targets

G protein-receptor binding interface: For designing neutralizing antibodies and small molecule inhibitors.

F protein fusion peptide region: To block viral entry.

P protein interferon antagonism domain: For developing immunomodulatory strategies.

Host receptor Ephrin-B2/B3 binding sites: To explore cross-species transmission mechanisms and predict host range.

Founded in Strasbourg, France, the abinScience brand leverages the region’s exceptional research and innovation ecosystem to focus on developing and producing high-quality life science reagents. Committed to the vision of “Empowering Bioscience Discovery”, abinScience provides efficient and reliable experimental solutions to support cutting-edge life science research worldwide. Below is a list of abinScience’s NiV-related proteins and antibodies:

Type Catalog No. Product Name
Protein VK631012 Recombinant Nipah virus/NiV G protein/Glycoprotein G Protein, N-His
VK521012 Recombinant Nipah virus/NiV F/Fusion glycoprotein F0 Protein, N-His-SUMO & C-Strep
VK521022 Recombinant Nipah virus/NiV F/Fusion glycoprotein F0 Protein, N-His
VK432012 Recombinant Nipah virus/NiV Protein N/Nucleoprotein Protein, N-His
VK432022 Recombinant Nipah virus/NiV Protein N/Nucleoprotein Protein, N-His-SUMO & C-Strep
VK408012 Recombinant Nipah virus/NiV M/Matrix Protein, N-His
Antibody VK685015 Anti-HeV/NiV Glycoprotein G Antibody (1A050)
VK685013 Anti-HeV/NiV Glycoprotein G Antibody (m102.3)
VK685023 Anti-HeV/NiV Glycoprotein G Antibody (m102.4)
VK685033 Anti-HeV/NiV Glycoprotein G Antibody (HENV-26)
VK685043 Anti-HeV/NiV Glycoprotein G Antibody (HENV-32)
VK685053 Anti-HeV/NiV Glycoprotein G Antibody (HENV-1)
VK685063 Anti-HeV/NiV Glycoprotein G Antibody (HENV-2)
VK685073 Anti-HeV/NiV Glycoprotein G Antibody (HENV-9)
VK685083 Anti-HeV/NiV Glycoprotein G Antibody (HENV-10)
VK685093 Anti-HeV/NiV Glycoprotein G Antibody (HENV-18)
VK685103 Anti-HeV/NiV Glycoprotein G Antibody (HENV-21)
VK685113 Anti-HeV/NiV Glycoprotein G Antibody (HENV-43)
VK521013 Anti-HeV/NiV F/Fusion glycoprotein F0 Antibody (mAb66)
VK431013 Anti-HeV/NiV F/Fusion glycoprotein F0 Antibody (5B3)
VK431023 Anti-HeV/NiV F/Fusion glycoprotein F0 Antibody (12B2)
VK431033 Anti-HeV/NiV F/Fusion glycoprotein F0 Antibody (1F5)
VK521010 InVivoMAb Anti-Nipah virus/NiV Prefusion Antibody (4H3)
VK521020 InVivoMAb Anti-Nipah virus/NiV Prefusion Antibody (1H8)
VK521030 InVivoMAb Anti-Nipah virus/NiV Prefusion Antibody (1A9)
VK631010 InVivoMAb Anti-Nipah virus/NiV G protein/Glycoprotein G Antibody (nAH1.3)
VK521040 InVivoMAb Anti-Nipah virus/NiV F/Fusion glycoprotein F0 Antibody (2D3)
VK521050 InVivoMAb Anti-Nipah virus/NiV Prefusion Protein Antibody (2B12)
VK521060 InVivoMAb Anti-Nipah virus/NiV Prefusion Protein Antibody (1H1)
VK521070 InVivoMAb Anti-Nipah virus/NiV Fusion glycoprotein/F Trimer Antibody (Fab92)
VK685010 InVivoMAb Anti-HeV/NiV Glycoprotein G Antibody (HENV-103)
VK685020 InVivoMAb Anti-HeV/NiV Glycoprotein G Antibody (HENV-117)
VK521023 Anti-Nipah virus/NiV Fusion glycoprotein F2 Antibody (11F10)
VK521033 Anti-Nipah virus/NiV Fusion glycoprotein F1 Antibody (5G7)
VK521043 Anti-Nipah virus/NiV Fusion glycoprotein F2 Antibody (6D3)
VK631020 InVivoMAb Anti-Nipah virus/NiV Glycoprotein G Antibody (SAA2190)
VK631030 InVivoMAb Anti-Nipah virus/NiV Glycoprotein G Antibody (SAA2191)
VK631040 InVivoMAb Anti-Nipah virus/NiV Glycoprotein G Antibody (SAA2192)
VK521053 Anti-Nipah virus/NiV Fusion glycoprotein Nanobody (DS90)
VK521063 Anti-HeV/NiV Fusion Protein Antibody (DS90)

 

Reference:
1. Madhukalya R, Yadav U, Parray HA, et al. Nipah virus: pathogenesis, genome, diagnosis, and treatment. Appl Microbiol Biotechnol. 2025;109(1):158. Published 2025 jul 1. doi:10.1007/s00253-025-13474-6

2. Emerging Human Viral Diseases, Volume II. https://doi.org/10.1007/978-981-97-4480-0

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