Influenza is a worldwide
plague caused by the influenza virus (IAV)
infection, which is initiated by specific recognition with
sialic acids on host cell surface. Bovine
lactoferrin (bLf) is a
sialoglycoprotein belonging to the
transferrin family, and it plays an important role in immune regulation. It also shows toxicity against
cancer cells and pathogenic microorganisms including bacteria, fungi, and virus. The purpose of this study is to assess the roles of the sialylated
glycans on bLf against IAV. To this end, bLf were first treated with
sodium periodate to destroy its sialylated
glycans. Then, the binding activity of native or desialylated bLf with various IAV was assessed by blotting assay. Finally, their ability to inhibit IAV attachment to host cells was analyzed in vitro. Our result showed that the sialylated
glycans on bLf were almost completely destroyed by
sodium periodate treatment. Furthermore, the binding activity of desialylated bLf to IAV and the ability to inhibit IAV mimics binding to MDCK cells were significantly reduced compared to that of native bLf. These results demonstrated that the sialylated
glycans on bLf could serve as competitive substrates to block IAV attachment to host cells during the early stages of
viral infection. Our findings make an important contribute for the fully understanding of the mechanism of bLf in the prevention of IAV
infections and their possible applications in
antiviral infection.