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Introduction: The H9N2 avian influenza virus is widely disseminated in poultry and poses a zoonotic threat, despite vaccination efforts. Mutations at residue 198 of hemagglutinin (HA) are critical for antigenic variation and receptor-binding specificity, but the underlying molecular mechanisms remain unclear. This study explores the molecular mechanisms by which mutations at the HA 198 site affect the antigenicity, receptor specificity, and binding affinity of the H9N2 virus.

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Background: Seasonal vaccination is the mainstay of human influenza prevention. Licensed influenza vaccines are regularly updated to account for viral mutations and antigenic drift and are standardised for their haemagglutinin content. However, vaccine effectiveness remains suboptimal.

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Influenza remains a persistent global health challenge, largely due to the virus' continuous antigenic drift and occasional shift, which impede the development of a universal vaccine. To address this, the identification of broadly neutralizing antibodies and their epitopes is crucial. Nanobodies, with their unique characteristics and binding capacity, offer a promising avenue to identify such epitopes.

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Influenza and Aging: Clinical Manifestations, Complications, and Treatment Approaches in Older Adults.

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Influenza, a highly contagious respiratory viral illness, poses significant global health risks, particularly affecting older and those with chronic health conditions. Influenza viruses, primarily types A and B, are responsible for seasonal human infections and exhibit a propensity for antigenic drift and shift, contributing to seasonal epidemics and pandemics. The severity of influenza varies, but severe cases often lead to pneumonia, acute respiratory distress syndrome, and multiorgan failure.

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