IAV H3 Specific Neutra™ Antibody Products

Accelerate Your IAV H3 Research!

Creative Biolabs provides IAV H3 antibodies to give you comprehensive solutions for your study and research. The antibody we provide is optimized and suitable for various applications encompassing Western blotting, ELISA, immunohistochemistry, and flow cytometry. Our key solutions include:

• High-specificity antibodies for accurate IAV H3 detection.
• Reliable reagents for consistent, reproducible results.
• Custom antibody development services.

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Introduction of IAV H3

The H3 subtype of influenza A viruses (IAVs) represent a persistent zoonotic threat, maintaining endemic circulation across human, porcine, and avian reservoirs while exhibiting episodic spillover into equine and domestic poultry populations. Pandemic emergence is contingent upon antigenically novel HA variants that evade preexisting humoral immunity—a trajectory accelerated by adaptive mutations enhancing dual receptor tropism and aerosol transmission efficiency. Classified as low-pathogenicity avian influenza viruses (LPAIVs), H3 strains paradoxically display extensive antigenic diversity, with phylogeographic analyses identifying nine H3NX reassortants.

Fig. 1 Structural simulation of the H3 avian influenza virus HA protein.^1,3

Ecological persistence is underpinned by subclinical avian infections, which impede outbreak recognition and foster cryptic adaptive evolution. Structural analyses of HA’s receptor-binding domain (RBD) reveal that Q226L/G228S substitutions rewire sialic acid topology, enabling cross-species receptor engagement. Cryo-EM studies further resolve how epistatic mutations (R62I, A144G, N145S) allosterically modulate HA’s RBD loops, amplifying binding avidity to human-type receptors. Such mutations, coupled with glycan-shifting indels in the HA1 globular head, potentiate zoonotic bridging.

Antibody against IAV H3

The hemagglutinin (HA) globular head serves as the primary target for vaccine-induced antibodies due to its immunodominant epitopes. However, rapid antigenic evolution within this domain drives recurrent seasonal outbreaks. Antigenic divergence is spatially organized: H1 HA features five hypervariable regions (Sa, Sb, Ca1, Ca2, Cb), while H3 HA contains five analogous sites (A–E). These regions exhibit accelerated mutation rates to evade antibody neutralization, contrasting with the phylogenetically conserved receptor-binding site (RBS)—a shallow pocket bounded by the 130-loop, 150-loop, 190-helix, and 220-loop.

Although the RBS’s functional constraint limits variability, its compact geometry (surface area <400 Ų) poses steric incompatibility for conventional antibodies, whose paratopes inevitably engage epitope-adjacent variable residues. Recent advances have identified rare broadly neutralizing antibodies (bnAbs) that overcome this limitation through two strategies: (1) CDR-H3 loop insertion into the RBS to engage invariant residues (e.g., W153, H183), and (2) quaternary interactions stabilizing the 220-loop in prefusion conformations. Structural analyses of bnAbs like 3I14 and H2214 reveal convergent evolutionary solutions to RBS targeting, leveraging somatic hypermutation to refine binding angles. These findings redefine HA’s vulnerability landscape, highlighting the RBS-proximal regions as tractable targets for universal vaccine design despite their evolutionary constraints.

Published Data

Fig. 2 The reactivities of different H3 isolates with the mAb 9F12.^2,3

A monoclonal antibody (mAb)-based sandwich ELISA platform was established for precise detection of H3 avian influenza virus (AIV). Hybridoma cells were generated through murine immunization with purified H3 AIV antigens followed by cell fusion. Clones were screened via hemagglutination inhibition (HI) assays, with top-performing candidates undergoing iterative subcloning. A stable hybridoma line (9F12) secreting IgG1κ mAbs specific to H3 AIV was isolated. Immunofluorescence and immunoblotting confirmed 9F12’s exclusive reactivity with H3 antigens, with no cross-recognition of heterosubtypic influenza strains.

The 9F12 mAb was subsequently deployed in a sandwich ELISA format, enabling targeted antigen detection. Following rigorous optimization, the assay demonstrated high specificity (no cross-reactivity with non-H3 subtypes) and sensitivity (detection limit: 1.2 ng/mL). Clinical validation across 120 field specimens revealed 98% concordance with viral culture outcomes. Thermal stability testing confirmed retained functionality after 30 freeze-thaw cycles or 72-hour storage at 25°C. This mAb-driven assay establishes a rapid (<3 hours), reliable diagnostic framework for H3 AIV surveillance, advancing preparedness against avian influenza outbreaks. Its operational simplicity and reproducibility position it as a scalable tool for high-throughput field deployment and pandemic mitigation.

Why Choose Us?

At Creative Biolabs, we provide premium IAV H3 antibodies and precision-driven services to empower groundbreaking research. Our distinct advantages ensure your projects thrive:

• Advanced Platforms: Utilize cutting-edge technologies like high-throughput screening and AI-guided protein engineering for antibodies with superior specificity and affinity.
• Tailored Solutions: Access fully customizable services—from epitope-focused antibody design to large-scale production—aligned with your experimental goals.
• Rigorous Quality Control: Each antibody undergoes stringent validation (ELISA, SPR, neutralization assays) to guarantee purity and batch-to-batch consistency.

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REFERENCES

1. Yu, Jiantao, et al. "Concern regarding H3-subtype avian influenza virus." Frontiers in Microbiology 14 (2023): 1327470.
2. Luo, Sisi, et al. "Production and identification of monoclonal antibodies and development of a sandwich ELISA for detection of the H3-subtype avian influenza virus antigen." AMB Express 10 (2020): 1-9.
3. Distributed under Open Access license CC BY 4.0, without modification.