Lactoferrin (LF) is an iron-binding protein from the transferrin family present in mucus secretions such as milk, tears, saliva, seminal and vaginal fluids and also found in several organs and blood. It is well known for having antibacterial, immunomodulatory and anti-inflammatory properties. Lactoferrin is also capable of inhibiting the replication of both DNA- and RNA-viruses. Studies indicate that LF inhibits infection of the host cell by directly binding to virus particles or by binding to target cell molecules that the virus uses as a receptor or co-receptor. Additionally, LF regulates the antiviral response of the immune system through stimulating cells which play an important role during the early phases of viral infection, e.g. natural killer cells, monocytes, macrophages and granulocytes. The use of lactoferrin as an antiviral drug has a promising future, especially in cases of patients with immunosupression.
Lactoferrin, an iron-binding glycoprotein, has been extensively studied for more than 60 years now. The structure of the protein with its antimicrobial peptides, as well as functions originating from the structure, is described in this review. The synthesis mechanisms and multiple activities of lactoferrin are also discussed, with a particular attention paid to the antimicrobial and bacteriostatic properties of this protein. One can assume that, owing to its numerous functions and important role played in the mammary gland immunity, lactoferrin is a protein crucial to immune response during mastitis. Lactoferrin can be also regarded as a potential therapeutic and immunomodulatory agent. Our review summarises the functions and applications of lactoferrin in the context of bovine mastitis.
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