In January 2026, a new outbreak of Nipah virus (Nipah virus, NiV) emerged in West Bengal, India. As of January 26, five confirmed cases have been reported, including several healthcare workers involved in patient care. This confirms the risk of nosocomial human-to-human transmission, and nearly 100 close contacts have been placed under urgent home quarantine. The news has raised global alarm. Neighboring countries such as Nepal and Thailand have swiftly strengthened border screening measures, with international airports in Phuket and Chiang Mai implementing thermal imaging temperature checks and travel history verification. The World Health Organization (WHO) has once again issued a public health alert, highlighting the virus’s 40%–75% fatality rate and its potential for a large-scale pandemic. Nipah virus is more insidious than Ebola, with an extremely high mortality rate, long incubation period, and zoonotic transmission. First identified in Malaysia in 1998, it causes annual winter outbreaks in Bangladesh and has been recorded multiple times in India—this is the tenth outbreak in West Bengal since 2018.

Figure 1. Timeline of Nipah virus outbreaks from 1998 to 2024
Nipah virus belongs to the Paramyxoviridae family, genus Henipavirus and is closely related to Hendra virus (HeV). It has a negative-sense single-stranded RNA genome approximately 18.2 kb in length, encoding six structural proteins and three non-structural proteins. The virion consists of an envelope, nucleocapsid, and various functional proteins. The core structural proteins include nucleoprotein (N), phosphoprotein (P), matrix protein (M), fusion protein (F), glycoprotein (G), and large polymerase (L). Each plays a critical role in viral replication, transmission, and pathogenesis, contributing to its high pathogenicity and transmissibility.
Figure 2. Schematic representation of Nipah virus structure and proteins
| Protein | Full Name | Function |
|---|---|---|
| Nucleoprotein N | Nucleocapsid protein | Encapsulates the viral RNA genome to form the nucleocapsid complex, protecting genetic material from host enzymes and directly participating in viral replication and transcription—an essential component of the viral life cycle. |
| Phosphoprotein P | Phosphoprotein | Acts as a cofactor for the large polymerase (L), stabilizing it. Through RNA editing, it generates V and W proteins that help the virus evade the host immune response. |
| Matrix protein M | Matrix protein | Links the nucleocapsid to envelope glycoproteins, providing structural support for virion assembly, mediating budding from host cells, and participating in viral morphogenesis via nucleocytoplasmic shuttling. |
| Fusion protein F | Fusion protein | Initially synthesized as an inactive F₀ precursor, it is cleaved into F₁ and F₂ subunits. It mediates fusion between the viral envelope and host cell membrane, a critical step for viral entry; conformational changes directly affect infection efficiency. |
| Glycoprotein G | Glycoprotein | Forms homotetramers that specifically bind host Ephrin-B2/B3 receptors, determining host range and tissue tropism. It serves as the “key” for viral entry and is the primary target for neutralizing antibodies. |
| Large polymerase L | Large polymerase | The core enzyme for replication and transcription (~250 kDa), containing RNA-dependent RNA polymerase and methyltransferase domains. It catalyzes mRNA synthesis and genome replication, essential for viral proliferation. |
The high pathogenicity of Nipah virus results from its unique infection mechanisms and immune evasion strategies, which together cause severe pathological damage:
Core Pathogenic Mechanisms of Nipah Virus
Figure 3. Nipah virus life cycle
No licensed vaccines or specific treatments exist for Nipah virus, but significant breakthroughs have been achieved in recent years:
Figure 4. NiV G-ferritin protects Syrian golden hamsters from lethal NiV Malaysia strain infection
Figure 5. Schematic of a one-step visual RT-RPA-CRISPR/Cas12 assay for NiV detection
Nipah virus outbreaks are concentrated in India and Bangladesh, primarily linked to consumption of date palm sap contaminated by fruit bats. Transmission also occurs directly from bats or via intermediate hosts such as pigs. The current West Bengal outbreak highlights diverse transmission routes, including foodborne, droplet, saliva, and human-to-human spread, with nosocomial infections among healthcare workers underscoring the risk.
The incubation period ranges from 4 to 14 days (up to 45 days), and asymptomatic carriers can transmit the virus, complicating control efforts. Strains vary in virulence; Indian and Bangladeshi strains (NiV-B) have fatality rates of 70%–100% and high human-to-human transmission (~75%), compared to the Malaysian strain (NiV-M, ~8%).
In 2022, a collaborative study published in the New England Journal of Medicine (NEJM) reported a new henipavirus—Langya virus (LayV)—isolated from febrile patients with animal contact in eastern China. The genome is similar to other henipaviruses. A total of 35 acute cases were identified (26 mono-infections), with no fatalities. No secondary transmission was observed among 15 close contacts of 9 patients, suggesting low human-to-human risk. Shrews are suspected as the natural reservoir.
Figure 6. Genetic and epidemiological features of LayV
Key Prevention Measures: Nipah virus has a high fatality rate (40%–75%), long incubation period (up to 45 days), and human-to-human transmission risk. With no specific vaccine or treatment available, core measures include strengthened border screening, avoiding contact with wildlife and contaminated food, and strict healthcare worker protection.
The emergence of new henipaviruses and recurrent Nipah outbreaks highlight ongoing zoonotic risks from bats and shrews. Current prevention focuses on border screening, avoiding wildlife contact and contaminated food, and proper healthcare worker protection.
In research, the G protein-receptor interface and F protein fusion peptide remain key targets for vaccines and therapeutics. Advances in clinical trials, new diagnostic tools, and studies on viruses like Langya are paving the way for a comprehensive prevention system against the henipavirus family. abinScience has developed recombinant G and F proteins as well as monoclonal antibodies to support fundamental research.
Below are the latest abinScience NiV-related recombinant proteins and antibodies. Catalog numbers link directly to product pages.
| Catalog No. | Product Name |
|---|---|
| VK631011 | Recombinant Nipah virus G protein/Glycoprotein G Protein, C-His |
| VK521011 | Recombinant Nipah virus/HeV F/Fusion glycoprotein F0 Protein, C-His |
| 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 |
| VK499012 | Recombinant Nipah henipavirus M/Matrix Protein, N-His |
| VK408012 | Recombinant Nipah virus/NiV M/Matrix Protein, N-His |
| VK078012 | Recombinant Nipah virus Phosphoprotein, N-His |
| VK631021 | Recombinant Nipah virus Glycoprotein, C-His |
| VK521042 | Recombinant Nipah virus Fusion Protein, N-GST&C-His |
| Catalog No. | Product Name |
|---|---|
| VK631010 | InVivoMAb Anti-Nipah virus/NiV G protein/Glycoprotein G Antibody (nAH1.3) |
| 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) |
| 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) |
| 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) |
| VK631014 | Anti-Nipah virus/HeV G protein/Glycoprotein G Polyclonal Antibody |
| VK521014 | Anti-Nipah virus/HeV F/Fusion glycoprotein F0 Polyclonal Antibody |
| VK432014 | Anti-Nipah virus/HeV Protein N/Nucleoprotein Polyclonal Antibody |
| VK408014 | Anti-Nipah virus M/Protein M Polyclonal Antibody |
| VK499014 | Anti-Nipah henipavirus M/Matrix protein Polyclonal Antibody |
| 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) |
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