Prophylaxis and therapy of pandemic H1N1 virus infection using egg yolk antibody.

Influenza A virus infects the human respiratory system and causes acute and fatal pulmonary diseases. The emergence of drug-resistant viral strains highlights the need for alternative therapeutic approaches. In this work, IgY antibody was raised in immunized laying hens, and its antiviral activity was evaluated in the context of passive immunization. With inactivated whole H1N1 virus, high-titer IgY antibody 9.18 mg/mL egg yolk was induced by the eighth week after immunization. Western blotting and the hemagglutination inhibition (HI) test demonstrated that the IgY antibody could specifically bind the neuraminidase and hemagglutinin of the H1N1 virus. In the plaque reduction assay, the IgY antibody reduced the H1N1 viral infection in MDCK (Madin-Darby canine kidney) cells. In a mouse model, the anti-H1N1 IgY antibody exhibited in vivo protection by reducing the infectious titer of the virus in the lung while maintaining the weight and normal structure of the lung tissue. Additionally, the anti-H1N1 IgY antibody exhibited protective activity comparable to the neuraminidase inhibitor oseltamivir. These results demonstrated that IgY can be easily produced and can offers an effective alternative approach for influenza control.

Preparation and characterization of egg yolk immunoglobulin Y specific to influenza B virus.

The aim of this study was to prepare egg yolk immunoglobulin (IgY) for use in the prevention and treatment of influenza B viral infections. Laying hens were immunized with inactivated influenza B virus (IBV), and IgY was isolated from the egg yolk by multiple polyethylene glycol (PEG) 6000 extraction and ammonium sulfate purification steps. The titers and specificity of the purified antibodies were assessed. The specific IgY titer increased beginning the second week after the first immunization, with the titer peaking at the fifth week. The yield of IgY was 76.5mg per yolk, and the purity was 98.2%. The use of western blotting and the hemagglutination inhibition (HI) test demonstrated that IBV-specific IgY binds specifically to influenza B virus proteins, and a plaque reduction assay revealed the neutralization efficacy of IBV-specific IgY at reducing influenza infection in MDCK cells. Furthermore, when mice were treated intranasally prior to or after influenza B virus infection, IBV-specific IgY protected the mice from influenza infection or reduced viral replication in their lungs, respectively. These findings indicate that IgY is an easily prepared and rich source of antibodies that offers a potential alternative strategy for preventing and treating influenza B infections.