HeV G & NiV G Specific Neutra™ Antibody Products

Are you struggling with prolonged timelines in antiviral drug development or challenges in targeting high-risk pathogens like Hendra and Nipah viruses? Creative Biolabs' HeV G and NiV G specific Neutra™ antibody products leverage advanced recombinant protein engineering and high-throughput epitope mapping to accelerate the development of potent, target-specific therapies, ensuring robust neutralization and reliable validation for critical research and clinical applications.

Introduction to HeV G and NiV G

Hendra virus (HeV) and Nipah virus (NiV), members of the Henipavirus genus within the Paramyxoviridae family, are zoonotic pathogens causing severe respiratory and neurological diseases in humans. The viral attachment glycoprotein (G protein) is essential for host cell entry, mediating receptor binding and membrane fusion. HeV G and NiV G share significant structural homology, targeting ephrin-B2/B3 receptors to initiate infection. Their high pathogenicity and pandemic potential underscore the urgency of developing therapeutics targeting these glycoproteins.

Fig.1 HeV/NiV genome and virion structure.^1,3

• Structure

The HeV G and NiV G proteins are type II transmembrane glycoproteins composed of a globular head domain, a flexible stalk, and a transmembrane anchor. The receptor-binding site is located in the head domain, and the stalk facilitates trimerization and coordination with the fusion (F) protein. Cryo-EM studies reveal that conformational shifts in the G protein head domain upon receptor binding trigger F protein activation, enabling viral entry. Mutations in key residues (e.g., NiV G Tyr581, HeV G Glu582) disrupt ephrin interactions, highlighting critical epitopes for antibody targeting.

• Related Signaling Pathways

HeV and NiV infections dysregulate host immune pathways, including interferon (IFN) signaling, which the viruses evade via STAT1/STAT2 interference. The G protein's receptor-binding activity further activates pro-inflammatory cytokines (e.g., IL-6, TNF-α), exacerbating vascular leakage and neurological damage. Therapeutic antibodies blocking G protein-receptor interactions can restore IFN responsiveness and mitigate inflammation, offering dual mechanisms of viral neutralization and immunomodulation.

• Pathologies

HeV and NiV infections are linked to encephalitis, severe respiratory distress, and multiorgan failure, with mortality rates exceeding 50%. Outbreaks in Southeast Asia and Australia highlight their public health threat, necessitating rapid diagnostic and therapeutic solutions.

Fig.2 Transmission pathways, pathogenesis, and laboratory diagnosis of HeV and NiV infections.^2,3

Applications of HeV G and NiV G Neutralizing Antibodies

• Diagnostic Assay Development

HeV G/NiV G-specific antibodies enable rapid antigen detection in clinical samples. ELISA and lateral flow assays using these antibodies identify viral antigens within hours, critical for outbreak containment and early patient triage.

• Therapeutic Candidate Screening

High-potency mAbs serve as benchmarks for evaluating small-molecule inhibitors or vaccine candidates. Competitive binding assays and pseudovirus neutralization platforms using antibodies streamline lead optimization.

• Passive Immunotherapy

Prophylactic or post-exposure administration of neutralizing antibodies reduces viral load and improves survival in animal models. Clinical trials for antibody cocktails (e.g., combining RBD and stalk-targeting mAbs) aim to minimize escape mutant emergence.

• Vaccine Efficacy Evaluation

Quantifying neutralizing antibody titers in vaccinated subjects validates vaccine immunogenicity. Surrogate neutralization assays using recombinant HeV/NiV G proteins paired with antibodies offer scalable, biosafe alternatives to live-virus testing.

Our Anti-HeV G and NiV G Antibodies

Creative Biolabs offers highly specific and reliable HeV G and NiV G Neutra™ antibodies to further antiviral research and treatment development. Engineered for critical applications—from diagnostics to immunotherapy—these antibodies are rigorously validated to accelerate your path from bench to bedside. Our neutralizing antibodies against HeV G and NiV G are pivotal for disrupting viral entry and curbing pathogenesis. High-affinity monoclonal antibodies (mAbs) targeting the receptor-binding domain (RBD) or stalk region prevent conformational activation of the F protein. For example, mAbs binding to the HeV G ephrin-binding pocket demonstrate cross-neutralization of NiV, while epitope-specific candidates exhibit picomolar affinity in vitro. These antibodies have been carefully tested for specificity, neutralizing titers, and batch consistency, supporting preclinical and clinical development.

Contact our scientific team today to discuss custom solutions for your HeV/NiV projects.

REFERENCES

1. Tripp, Melanie N., et al. "The intracellular virus-host interface of henipaviruses." Journal of Virology (2025): e00770-25. https://doi.org/10.1128/jvi.00770-25
2. van den Hurk, Shaun, Aurelle Yondo, and Binu T. Velayudhan. "Laboratory Diagnosis of Hendra and Nipah: Two Emerging Zoonotic Diseases with One Health Significance." Viruses 17.7 (2025): 1003. https://doi.org/10.3390/v17071003
3. Distributed under Open Access license CC BY 4.0, without modification.