IAV HA Specific Neutra™ Antibody Products

Are you struggling with prolonged timelines in neutralizing antibody screening or inconsistent results in influenza therapeutics? Creative Biolabs' IAV HA-specific Neutra™ antibody products overcome these hurdles by leveraging advanced structural biology insights and high-throughput affinity maturation, enabling rapid identification of potent neutralizers to streamline antiviral drug and vaccine development.

Introduction to IAV HA

Influenza A virus hemagglutinin (IAV HA) is a glycosylated surface protein essential for viral entry into host cells. As the primary antigenic determinant of influenza A, HA mediates receptor binding and membrane fusion, driving viral infectivity. Its high mutation rate contributes to antigenic drift and shift, necessitating continuous surveillance for emerging strains.

• Structural Features

IAV HA exists as a homotrimer, each monomer comprising a globular head (HA1) and a stalk (HA2). The HA1 domain harbors the receptor-binding site (RBS) for sialic acid on host cells, while HA2 facilitates pH-dependent membrane fusion. Structural flexibility in the RBS allows adaptation to avian or mammalian hosts, whereas conserved epitopes in the stalk region are targets for broadly neutralizing antibodies. Cryo-EM studies reveal conformational changes during fusion, informing therapeutic designs that block viral entry.

• Related Signaling Pathways

HA engagement triggers clathrin-mediated endocytosis, followed by endosomal acidification, which activates HA2-mediated membrane fusion. This process intersects with host pathways like the interferon (IFN) response, where HA's antagonism of IFN production enhances viral replication. Additionally, HA binding modulates ER stress pathways, influencing apoptosis and immune evasion.

Fig.1 The IAV endocytosis and HA conformational change.¹

• Associated Pathologies

IAV HA is central to seasonal and pandemic influenza outbreaks, causing respiratory illnesses marked by fever, cough, and pneumonia. Severe cases progress to acute respiratory distress syndrome (ARDS), particularly in high-risk populations. The 1918 H1N1 and 2009 H1N1 pandemics underscore HA's role in viral pathogenicity and global health crises.

Applications of IAV HA-Specific Neutralizing Antibodies

• Vaccine Development and Efficacy Testing

HA-specific antibodies serve as critical benchmarks for evaluating vaccine immunogenicity. By mapping antigenic sites, these tools guide the optimization of HA-based vaccines to enhance breadth and durability against evolving strains.

• Therapeutic Antibody Development

Neutralizing mAbs targeting conserved HA epitopes are promising candidates for universal influenza therapies. Preclinical studies demonstrate their ability to reduce viral load and severity in animal models, supporting rapid translation to clinical trials.

• Diagnostic Assay Development

Anti-HA antibodies enable rapid detection of circulating strains in clinical samples via ELISA or lateral flow assays. Their high specificity ensures accurate serological profiling to monitor outbreaks and vaccine coverage.

• Mechanism of Action Studies

These antibodies are vital for dissecting HA's structural dynamics during fusion. Applications include cryo-EM studies to visualize antibody-antigen interactions and functional assays to identify resistance mutations.

Our Anti-IAV HA Antibody Products

Neutralizing antibodies targeting HA block receptor binding or fusion, offering dual mechanisms for viral inhibition. High-affinity monoclonal antibodies (mAbs) against the HA stalk confer cross-protection across subtypes (e.g., H1, H3), while head-targeting mAbs neutralize strain-specific variants. Creative Biolabs' antibodies are validated for epitope specificity, stability across pH gradients, and compatibility with neutralization assays, making them indispensable for vaccine design and therapeutic development.

Creative Biolabs provides IAV HA-specific Neutra™ antibody portfolio combining cutting-edge bioengineering with rigorous validation to empower your antiviral research. Our antibodies are optimized for neutralization potency, batch consistency, and cross-reactivity profiling.

Contact our team today to discuss your project requirements and explore how our solutions can accelerate your timeline.

REFERENCE

1. Hwang, Hye Suk, Mincheol Chang, and Yoong Ahm Kim. "Influenza–host interplay and strategies for universal vaccine development." Vaccines 8.3 (2020): 548. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/vaccines8030548