H5N1 Specific Neutra™ Antibody Products

Creative Biolabs provides a comprehensive solution for IAV subtype H5N1 antibody products and services to support your research applications, from basic study to diagnostic development. Our expertise and high-quality products ensure that your project progresses smoothly and efficiently.

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Introduction of IAV subtype H5N1

The etiological agent of ongoing global avian epizootics, HPAI A/H5N1, persists as an entrenched pathogen within avian reservoirs (Galliformes, Anseriformes) while demonstrating panzootic spillover into 37 mammalian taxa, including humans. Its sustained endemicity in poultry systems across Southeast Asia and Africa arises from recombination-driven antigenic drift and wild bird-mediated dissemination along the Central Asian Flyway. Zoonotic transmission occurs via exposure to virions shed in cloacal secretions or aerosolized respiratory droplets, with human infections exhibiting a case-fatality ratio (CFR) of 59% (667 cases, 17 nations; 2003-2023 WHO data).

Fig.1 H5N1 transmission cycle.^1,3

Notably, H5N1’s PB2-E627K polymorphism enhances mammalian airway replication (Δlog₁₀ viral load = 2.7 in ferret models), while its HA protein maintains preferential binding to avian-type α2,3-linked sialic acid receptors—a dual-host tropism that facilitates intermittent cross-species transmission without sustained human adaptation. Despite prophylactic culling of 5.2×10⁸ domestic birds, viral reseeding persists via migratory waterfowl (e.g., Anas platyrhynchos) acting as asymptomatic carriers, enabling transcontinental spread to 64 countries. Recent isolates from bovine lacteal secretions (2024 U.S. outbreaks) underscore expanding host plasticity, heightening pandemic risk should HA acquire human-adapted α2,6-SA binding via Q226L/G228S substitutions.

Antibody against IAV subtype H5N1

Hemagglutinin (HA), the principal influenza A virus surface glycoprotein, orchestrates viral tropism through bipartite functionality: receptor-mediated attachment via its HA1 globular head and pH-triggered membrane fusion governed by the HA2 stem. Proteolytic processing of the HA0 precursor yields disulfide-linked HA1/HA2 heterodimers, trimerized into metastable prefusion spikes. Immunodominant epitopes localize to HA1’s membrane-distal antigenic sites (Sb, Ca1, Ca2)—epicenters of adaptive evolution driven by immune selection—whereas cryptic conserved residues within the HA1-HA2 stem interface exhibit lower mutational tolerance. The stem-directed monoclonals, exemplified by CR6261 and FI6v3, exhibit pan-H1/H3/H5 neutralization by sterically inhibiting HA’s pH-dependent conformational rearrangement. Antibody-mediated interference with either receptor engagement (globular domain) or fusion machinery (stem region) underscores HA’s dual vulnerability to humoral immunity.

Mechanistically, stem-binding MAbs inhibit HA’s pH-dependent conformational rearrangements critical for endosomal escape, while select head-targeting clones sterically hinder receptor engagement. This dual vulnerability—disrupting either viral attachment or fusion—underscores HA’s centrality in therapeutic antibody development against antigenically plastic influenza variants.

Published Data

Fig. 2 IgY protects against H5N2 virus attack.^2,3

This study demonstrates the cross-clade protective efficacy of avian IgY antibodies derived from commercially sourced poultry eggs against highly pathogenic avian influenza (HPAI) H5N1 and antigenically related H5N2 strains in murine models. Prophylactic and therapeutic intranasal administration of H5-specific IgY suppressed pulmonary viral titers and achieved full clinical recovery, with 100% survival in lethal challenge paradigms. Parallel evaluation of H1N1-specific IgY—generated through hen immunization with β-propiolactone-inactivated H1N1 (A/PR8)—exhibited neutralizing capacity against contemporary pandemic H1N1/09 variants, confirming platform versatility.

Mechanistic profiling revealed IgY-mediated blockade of hemagglutinin-receptor engagement alongside Fc-mediated phagocytic activation, synergizing to limit viral dissemination. The immediate availability and scalable production of preformulated H5N1-specific IgY position it as a pragmatic passive immunotherapy for pandemic preparedness, particularly in regions at high risk of zoonotic spillover events.

Why Choose Us?

Creative Biolabs is your trusted partner for IAV subtype H5N1 antibody solutions. With cutting-edge technology, extensive expertise and a commitment to quality, we are dedicated to providing superior products and services. Our key advantages include:

• State-of-the-art Platforms: including high-throughput screening, advanced protein purification, and sensitive characterization assays.
• Customization: We tailor our services to the unique needs of each project.
• Cost-effective: We provide cost-effective solutions and project management to meet your goals and budget.

FAQs

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REFERENCE

1. Imperia, Elena, et al. "Avian influenza: could the H5N1 virus Be a potential next threat?." Microbiology Research 14.2 (2023): 635-645.
2. Nguyen, Huan H., et al. "Prophylactic and therapeutic efficacy of avian antibodies against influenza virus H5N1 and H1N1 in mice." PloS one 5.4 (2010): e10152.
3. Distributed under Open Access license CC BY 4.0, without modification.