H13N9 NA Specific Neutra™ Antibody Products

Are you currently facing significant hurdles in your avian influenza studies, such as high background noise in inhibition assays, difficulties in differentiating rare serotypes like H13N9, or a lack of reliable reagents for structural validation? Creative Biolabs' anti-H13N9 NA specific Neutra™ antibody products help you achieve superior experimental accuracy and accelerate your therapeutic discovery timeline through our proprietary high-affinity screening platform and rigorous functional validation protocols.

Introduction to H13N9 NA

The Influenzavirus A Subtype H13N9 Neuraminidase (H13N9 NA) is a critical surface glycoprotein embedded within the viral envelope of the H13N9 influenza virus. Primarily isolated from aquatic bird reservoirs, particularly gulls and shorebirds, H13N9 NA belongs to the N9 lineage of neuraminidases. As a Type II integral membrane protein, it functions as a specialized glycosyl hydrolase that is indispensable for the viral life cycle, serving as the primary engine for viral egress and dissemination within the host.

Fig.1 Phylogenetic analysis of H13N9 avian influenza viruses (AIVs).¹

• Structure

The functional architecture of H13N9 NA is characterized by a homotetrameric configuration, forming a prominent "mushroom-shaped" head atop a slender, flexible stalk. Each monomeric unit comprises a cytoplasmic tail, a transmembrane domain, a stalk, and a large globular head. The head domain serves as the catalytic powerhouse, containing the enzymatically active site, a highly conserved pocket stabilized by a network of triarginine residues and acidic amino acids. This site is surrounded by hypervariable loops that define the specific antigenic identity and "escape" potential of the H13N9 subtype. The tetrameric stability is essential for maintaining the correct orientation of the catalytic site relative to the host cell membrane.

• Function

The primary biochemical role of H13N9 NA is the hydrolytic cleavage of terminal alpha-linked sialic acid residues from host cell glycoproteins and glycolipids. This enzymatic activity is multi-faceted: it allows the virus to penetrate the dense, sialic acid-rich mucus layers of the respiratory and intestinal tracts; it prevents the self-aggregation of newly synthesized progeny virions; and most critically, it severs the bond between viral hemagglutinin and host receptors, facilitating the release of the virus into the extracellular environment to infect adjacent cells. Without efficient H13N9 NA function, the viral replication cycle is effectively halted at the final stage of budding.

• Related Signaling Pathways
  H13N9 NA activity significantly modulates the host's biochemical signaling landscape through several mechanisms:
  • Immune Evasion Signaling: By desialylating cell surface receptors, H13N9 NA can uncover cryptic epitopes or alter the binding affinity of host immune receptors like Siglecs, suppressing innate immune recognition.
  • Pro-inflammatory Cascade: The enzymatic release process triggers the activation of the MAPK and NF-κB pathways, leading to an up-regulation of pro-inflammatory cytokines such as IL-6 and TNF-α.
  • Apoptotic Modulation: Intense NA activity can influence cellular stress responses, potentially modulating programmed cell death pathways to favor viral replication windows.
  • Tlr-Mediated Recognition: Alterations in the glycosylation patterns on the cell surface can impact the sensitivity of Toll-like receptors (TLRs), affecting the downstream antiviral state of the host cell.
• Related Diseases

H13N9 NA is a central determinant in the pathogenesis of Avian Influenza. While typically associated with low-pathogenic infections in wild bird populations, the threat of genetic reassortment remains constant. Zoonotic transmission can lead to severe respiratory distress, pneumonia, and systemic inflammatory complications in secondary hosts, making it a priority for pandemic surveillance and the study of cross-species transmission barriers.

Applications of H13N9 NA Neutralizing Antibodies

• Therapeutic Viral Spread Inhibition

The most vital application is the capacity to halt viral replication cycles. By binding to the enzymatic head domain, these antibodies provide steric hindrance that physically obstructs the active site from accessing sialic acid substrates, trapping the virus on the surface of the primary infected cell.

• High-Fidelity Subtype Identification

In clinical and epidemiological diagnostics, these antibodies are indispensable for the precise identification of influenza strains. Their exceptional specificity allows researchers to differentiate H13N9 from other co-circulating N9 or N1 lineage viruses that might produce cross-reactive signals in generic assays.

• Vaccine Immunogenicity Standardization

As the industry moves toward neuraminidase-based vaccine candidates, these antibodies serve as "gold standard" reagents for profiling immune responses. They are utilized in Enzyme-Linked Lectin Assays (ELLA) to quantify functional antibody titers in clinical trial subjects.

• Structural Epitope Mapping

In structural biology, these antibodies are used to identify "sites of vulnerability" on the H13N9 NA tetramer. Through X-ray crystallography or Cryo-EM, they stabilize specific protein conformations, allowing for atomic-level mapping of the antibody-antigen interface to guide rational vaccine design.

• Passive Immunotherapy Research

Neutralizing antibodies are being explored as immediate-acting prophylactic agents for high-risk populations. Unlike vaccines, which require time to develop immunity, Anti-H13N9 NA antibodies provide immediate passive protection, which is critical for frontline workers during avian outbreaks.

• Antiviral Drug Resistance Monitoring

These antibodies are essential tools for monitoring the emergence of drug-resistant viral variants. By comparing inhibitory profiles against wild-type and mutant NA, researchers can characterize how specific mutations affect both enzymatic function and antibody binding.

Our Anti-H13N9 NA Antibodies

Creative Biolabs provides an industry-leading portfolio of Neutra™ antibodies specifically targeting the H13N9 NA, meticulously developed to support high-stakes virology research. Our catalog includes a diverse range of monoclonal antibodies (mAbs) and recombinant formats that exhibit picomolar affinity for the H13N9 NA glycoprotein, ensuring unmatched sensitivity in complex biological matrices.

• Broad Analytical Versatility: Our H13N9 NA antibodies are strictly validated for a wide array of high-impact applications, including Enzyme-Linked Immunosorbent Assay (ELISA), Western Blot (WB), Flow Cytometry (FC), and Immunofluorescence (IF).
• High-Potency Neutralization: Specifically screened for functional interference, our Neutra™ series demonstrates superior performance in Neuraminidase Inhibition (NI) assays, effectively blocking the enzymatic release of viral progeny.
• Optimized for Subtyping: Engineered to recognize unique epitopes within the N9 lineage, these reagents allow for the clear differentiation of H13N9 from N1-N8 subtypes, eliminating cross-reactivity concerns in surveillance studies.
• Customized Production Scales: To accommodate transition from pilot studies to large-scale screening, we offer flexible production options, including biotinylation, fluorophore conjugation, and bulk-scale recombinant expression under stringent quality control.

Creative Biolabs is your trusted partner for high-quality anti-H13N9 NA specific neutra™ antibody products, providing the specialized precision required for groundbreaking viral research and therapeutic development. We are dedicated to supporting your projects with superior reagents and expert technical insights to ensure your success in combating avian influenza and advancing global health.

Ready to accelerate your research? Contact our team to learn more and discuss your project.

Reference

1. Meng, Bo, et al. "Evolutionary Events Promoted Polymerase Activity of H13N8 Avian Influenza Virus." Viruses 16.3 (2024): 329. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/v16030329