H7N9 Specific Neutra™ Antibody Products

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Creative Biolabs deliver high-quality, reliable Influenza A Virus H7N9 antibodies to support your research and development projects. We help you develop highly specific antibodies through innovative protein engineering techniques. Our antibodies provide the specificity and sensitivity you need for accurate and reproducible results.

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Introduction of IAV virus H7N9

First identified in 2013 during zoonotic spillover events, influenza A/H7N9 represents an avian-origin virus with low pathogenicity in avian reservoirs but marked virulence in humans, often precipitating severe lower respiratory tract infections. Central to its infectivity is the hemagglutinin (HA) surface glycoprotein, a trimeric class I fusion machinery that orchestrates viral entry through biphasic functionality. These insights into HA’s antigenic landscape and vulnerability to structural inhibition directly inform rational vaccinology.

Fig. 1The influenza A virus (IAV) and its viral genome. (OA Literature) Fig. 1 Diagram of the influenza A virus (IAV) and its viral genome.1,3

Antibody against IAV Virus H7N9

Antibodies targeting the H7N9 hemagglutinin (HA) glycoprotein mediate viral neutralization through steric occlusion of its receptor-binding domain (RBD), a conformational strategy that impedes α2,3-sialylated glycan recognition—a prerequisite for host cell internalization. Structural virology studies delineate that neutralization potency correlates with antibody paratope occupancy of conformationally labile HA1 epitopes, particularly within the RBD’s 130-loop, where spatial competition destabilizes sialic acid coordination geometries critical for viral endocytosis.

HA-specific monoclonal antibodies (mAbs) elicit heterosubtypic immunity in murine and ferret models, neutralizing antigenically distinct H7N9 clades through dual mechanisms: RBD blockade and FcγRIIIa-dependent phagocyte activation. Their bifunctional utility extends beyond therapy, serving as sentinel tools for antigenic cartography via epitope-resolved ELISA and pseudovirus neutralization assays, which track HA’s evolutionary drift. These mAbs further benchmark vaccine candidates by quantifying immunogen fidelity to conserved HA stem epitopes, a metric predictive of cross-clade efficacy.

The strategic development of such biologics addresses critical gaps in pandemic responsiveness. Deployable within weeks of outbreak emergence, HA-directed mAbs disrupt transmission networks at zoonotic interfaces while reducing case-fatality rates through early viremia suppression—an advantage over strain-matched vaccines requiring months for development. This multifunctionality positions them as cornerstone countermeasures against H7N9’s pandemic potential, particularly given its propensity for immunological escape via RBD-focused antigenic drift.

Published Data

Fig. 2 Anti-H7 human monoclonal antibodies inhibit H7N9 virus. (OA Literature) Fig. 2 Anti-H7 human monoclonal antibodies inhibit H7N9 virus through multiple mechanisms.2,3

H7-reactive human mAb responses that persist for months after infection were investigated using H7-reactive mAbs isolated from human peripheral blood memory B cells obtained approximately 11 months after natural infection with H7N9. The data demonstrated that memory B cell-derived mAbs exhibited greater cross-reactivity to heterologous H7 HAs compared with antibodies isolated early after infection or vaccination. Most head domain-targeting mAbs isolated 11 months after infection retained reactivity to all H7Nx viruses Most of the mAbs targeting the head domain, which was isolated 11 months after infection, retained reactivity to all H7Nx viruses. These H7Nx viruses were tested in a panel representing all H7 virus lineages described. These studies suggest that natural infection with H7N9 and vaccination induce similar B cell repertoires. The mAbs showed broad cross-reactivity between H7 and H15 subtypes and were able to neutralize the virus through multiple mechanisms. These mAbs were induced by naturally occurring H7N9 infection in humans.

Why Choose Us?

Creative Biolabs is committed to providing highest-quality Influenza A Virus H7N9 antibodies products antibody service.

  • Uncompromising Quality: Dedicated to providing antibody products with high-standard quality.
  • Technical Expertise: Expertise in antibody development with our state-of-the-art facilities, ensures to meet your various research needs.
  • Customization Options: Whether you need antibodies for a specific application, isotype, or affinity, we can deliver a suitable solution.
  • Good Collaboration: We will work closely with you throughout the entire process, providing regular updates, seeking feedback, and addressing any concerns promptly.

FAQs

Q1: Can Creative Biolabs develop H7N9 antibodies for my specific research application?

A1: Yes, Creative Biolabs offers custom antibodies suited to your specific experiment requirements.

Q2: What technical support will Creative Biolabs provide?

A2: Creative Biolabs offers comprehensive technical support to assist you with your experiments. Our scientists can answer your questions and guide antibody usage and optimization.

Q3: Are there any discounts for bulk orders?

A3: Yes, Creative Biolabs offers competitive pricing and discounts for bulk orders. Reach out to our sales team to receive a quote.

For more information about Creative Biolabs' IAV virus H7N9 antibodies and services, please contact us.

REFERENCES

  1. Bisset, Andrew T., and Gerard F. Hoyne. "Evolution and adaptation of the avian H7N9 virus into the human host." Microorganisms 8.5 (2020): 778.
  2. Gilchuk, Iuliia M., et al. "Human antibody recognition of H7N9 influenza virus HA following natural infection." JCI insight 6.19 (2021): e152403.
  3. Distributed under Open Access license CC BY 4.0, without modification.
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Anti-IAV H7N9 Neutralizing Antibody (V3S-0622-YC293) (CAT#: V3S-0622-YC293)

Target: IAV H7N9

Host Species: Human

Target Species: Influenzavirus A subtype H7N9,

Application: ELISA,Neut,FuncS,

For research use only, not directly for clinical use.


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