Bovine lactoferrin (bLF)

Bovine lactoferrin (bLF) is a multifunctional 80 kDa iron-binding glycoprotein belonging to the transferrin family, predominantly found in bovine milk and mucosal secretions (UniProt P02753). The molecule is organized into two symmetrical globular lobes, the N-lobe and the C-lobe, each containing a high-affinity binding site for one ferric (Fe3+) ion, which remains stable even under acidic conditions (PubMed: 21835141). As a critical component of the innate immune system, bLF provides broad-spectrum protection against bacteria, viruses, and fungi by sequestering essential iron and directly destabilizing pathogen membranes (PubMed: 16261256). In therapeutic contexts, bovine lactoferrin is utilized to enhance iron absorption in patients with anemia and to reduce the incidence of sepsis and necrotizing enterocolitis in neonates (PubMed: 28933417). It also demonstrates significant anti-inflammatory properties by modulating the expression of cytokines like TNF-alpha and IL-6 through receptor-mediated signaling pathways. Due to its high homology with human lactoferrin and its Generally Recognized as Safe (GRAS) status, it is widely used in clinical nutrition and as an adjunct therapy for chronic inflammatory and infectious diseases.

Other names

LactotransferrinBovine lactotransferrinHolo-lactoferrinIron-binding glycoprotein

Bovine lactoferrin functions primarily through the high-affinity sequestration of ferric iron, which deprives pathogenic microorganisms of a vital nutrient required for growth and replication. It also exerts direct bactericidal effects through its N-terminal domain, which can be cleaved to form lactoferricin, a peptide that disrupts microbial cell membranes. Furthermore, it acts as an immunomodulator by binding to specific host receptors such as LRP1 and Intelectin-1, thereby regulating the production of pro-inflammatory cytokines and the activity of natural killer cells and macrophages.