Binding Characteristics of Bovine Lactoferrin to the Cell Surface ofClostridiumSpecies and Identification of the Lactoferrin-binding Protein

Identification of lactoferrin-binding proteins inStreptococcus dysgalactiaesubsp.dysgalactiaeandStreptococcus agalactiaeisolated from cows with mastitis

“…Since Lf concentration is relatively high in bovine mammary secretions and Lf binds to mammary epithelial cells [10,11], bacterial binding of Lf has been considered to have a role in the pathogenesis of bovine mastitis. Bovine Lf has been reported to bind to the cell surface of Clostridium species [12], coagulase‐negative Staphylococcus species [13], Staphylococcus aureus [14], S. agalactiae [15,16], and Streptococcus uberis [17]. Studies conducted in our laboratory showed that S. uberis had two major lactoferrin‐binding proteins (LBPs) [17].…”

Identification of lactoferrin-binding proteins in Streptococcus dysgalactiae subsp. dysgalactiae and Streptococcus agalactiae isolated from cows with mastitis

“…dysgalactiae (S. dysgalactiae), are more resistant to the antibacterial e¡ects of Lf than Gram-negative bacteria [8,9], probably because of their low requirement for iron. Bovine Lf has been reported to bind to the cell surface of Clostridium species [12], coagulase-negative Staphylococcus species [13], Staphylococcus aureus [14], S. agalactiae [15,16], and Streptococcus uberis [17]. Bovine Lf has been reported to bind to the cell surface of Clostridium species [12], coagulase-negative Staphylococcus species [13], Staphylococcus aureus [14], S. agalactiae [15,16], and Streptococcus uberis [17].…”

“…Since Lf concentration is relatively high in bovine mammary secretions and Lf binds to mammary epithelial cells [10,11], bacterial binding of Lf has been considered to have a role in the pathogenesis of bovine mastitis. Bovine Lf has been reported to bind to the cell surface of Clostridium species [12], coagulase-negative Staphylococcus species [13], Staphylococcus aureus [14], S. agalactiae [15,16], and Streptococcus uberis [17].…”

The antimicrobial activity of proteins/peptides against antibiotic-resistant and -susceptible bacteria

“…This blister formation against E. coli, S. enterica serovar Typhimurium, and S. montevideo occurred at 20 |iM of lactoferrin and was dependent on Ca ++ , Mg% and Fe w concentrations in vitro (Yamauchi et al, 1993). Lactoferrin has been shown in vitro to also kill Helicobacter pylori at .5 mg lactoferrin/mL of solution and can also kill Clostridium perfringens, which is in part due to its iron-binding properties (Dial et al, 1998;Tomita et al, 1998). The killing activity on bacteria also occurred at the same concentration when lactoferrin was converted in vitro to lactoferricin by digestion using pepsin, trypsin, or chymotrypsin (Yamauchi et a., 1993).…”

“…CAUTION -some peptides (e.g., lysozyme) do not retain antimicrobial activity after multiple thawings a Data represents the concentrations of the antimicrobial protein/peptide that have been reported to kill specific Gram-positive and Gramnegative bacteria. Data summarized from the following publications, Bellamy et al, 1992;Dial et al, 1998;Ganz et al, 1990;Hughey and Johnson, 1987;Jones et al, 1994;Tomita et al, 1998;Yamauchi et al, 1993. b No effect (NE) on the organism reported.…”