Inhibition of bacteria by lactoferrin and other iron-chelating agents

Oram, J. D.; Reiter, B.

doi:10.1016/0304-4165(68)90015-9

Cited by 282 publications

(119 citation statements)

References 20 publications

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“…Since lactoferrin is a powerful chelator of iron (2, 6, 7) as well as of copper (8), it is tempting to speculate that this protein may be a valuable adjunct of lysozyme in the defense against bacterial invasion. Moreover, lactoferrin is by itself endowed with bacteriostatic properties which it owes to its iron-chelating capacity (21,23,28). It would also be interesting to clarify the possible relationship of lactoferrin with "phagocytin", the antimicrobial factor from polymorphonuclear leukocytes described by Hirsch (20).…”

Section: Discussionmentioning

confidence: 99%

Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

Masson¹,

Heremans²,

Schonne³

1969

The Journal of Experimental Medicine

655

295

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Lactoferrin, an iron-binding protein previously shown to occur in many external secretions, is identified as one of the major proteins present in human and guinea pig neutrophilic polymorphonuclear leukocytes. The identification of this protein in leukocyte extracts was based upon a comparison of its electrophoretic, antigenic, and iron-combining properties with the corresponding properties of the same protein isolated from human and guinea pig milk. Immunochemical quantitations showed that lactoferrin occurs in human neutrophilic leukocytes at the concentration of 3 µg per 106 cells. Tissue cultures from guinea pig bone marrow and spleen actively synthesized the protein, as shown both by net production of lactoferrin and incorporation of labeled amino acids into the protein. Immunohistochemical data indicate that lactoferrin first appears in myeloid cells at the stage of the promyelocyte.

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Section: Discussionmentioning

confidence: 99%

Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

Masson¹,

Heremans²,

Schonne³

1969

The Journal of Experimental Medicine

655

295

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“…Lactoferrin and transferrin, the iron binding proteins found in milk, have a bacteriostatic effect on the growth of Escherichia coli by depriving the bacteria of iron (Oram & Reiter, 1968). Milk antibody, which alone has no effect on the growth rate of bacteria, increases the bacteriostatic effect of lactoferrin or transferrin.…”

Section: Introductionmentioning

confidence: 99%

Bacteriostasis ofEscherichia coliby milk: IV. The bacteriostatic antibody of human milk

Dolby¹,

Honour²

1979

J. Hyg.

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summaryBacteriostatic activity for milk-sensitive and milk-resistant strains of Escherichia coli is reduced when IgA is removed from milk by precipitation. Lysozyme is not involved in bacteriostasis and can be removed without loss of activity; heavy bentonite absorption however removes some lactoferrin causing partial loss of activity.The heat-labile antigen eliciting bacteriostatic antibody for E. coli is present in milk-sensitive and milk-resistant strains and in some other Enterobacteriaceae, e.g. salmonella; it cross reacts with the antigen in others, e.g. proteus and enterobacter. The antibody is therefore likely to be present in all human milk as a result of the normal commensal gut flora and with widespread activity.

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“…An impressive plethora of roles have been attributed to LF including antimicrobial activity against bacteria, virus, yeast and parasitic protozoa, among others [15,16]. The mechanism underlying LF antibacterial activity is primarily ascribed to its iron chelating property which prevents the development of pathogenic bacteria, exerting a bacteriostatic effect [17,18]. Moreover, LF is able to bind to several bacterial surface components (proteins, lipotheichoic acid, porins, lipids) destabilizing the membrane polarity, hence increasing the permeability and metabolic burden of sensitive bacteria while preventing adhesion and invasion of host cells by a wide scope of bacteria [16,19].…”

Section: Introductionmentioning

confidence: 99%

“…Further, the bLF may exert a bacteriostatic activity due to its potent iron binding capacity that may deprive the environment of this essential micronutrient, blocking several essential biochemical reactions [17,18].…”

Section: Introductionmentioning

confidence: 99%

Antibacterial performance of bovine lactoferrin-fish gelatine electrospun membranes

Padrão

Machado

Casal

et al. 2015

International Journal of Biological Macromolecules

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The increase of antibiotic resistant microorganisms urged the development and synthesis of novel antimicrobial biomaterials to be employed in a broad range of applications, ranging from food packaging to medical devices. This work describes the production and characterization of a protein-based electrospun fibrous membranes bearing antimicrobial properties. Its composition is exclusively comprised of proteins, with fish gelatine as structural matrix and bovine lactoferrin (bLF) as the active antimicrobial agent. The bLF bactericidal effect was determined against clinical isolates of Escherichia coli and Staphylococcus aureus through microdilution assays. Two distinctive methods were used to incorporate bLF into the fish gelatine nanofibres: (i) as a filler in the electrospinning formulation with concentrations of 2, 5 and 10 (wt%), and cross-linked with glutaraldehyde vapour, in order to achieve stability in aqueous solution; and (ii) through adsorption in a solution with 40mgmL -1 bLF. Fourier transform infrared spectroscopy analysis showed that the structure of both proteins remained intact through the electrospinning blending and cross-linking procedure. Remarkable antibacterial properties were obtained with membranes containing 5% and 10% bLF with a bacterial reduction of approximately 90% and 100%, respectively. and 10 (%wt), and cross-linked with glutaraldehyde vapour, in order to achieve stability in aqueous solution; and ii) through adsorption in a solution with 40 mg mL -1 bLF. Fourier transform infrared spectroscopy analysis showed that the structure of both proteins remained intact through the electrospinning blending and cross-linking procedure. Remarkable antibacterial properties were obtained with membranes containing 5% and 10% bLF with a bacterial reduction of approximately 90% and 100%, respectively.

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Inhibition of bacteria by lactoferrin and other iron-chelating agents

Cited by 282 publications

References 20 publications

Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

Lactoferrin, an Iron-Binbing Protein Ni Neutrophilic Leukocytes

Bacteriostasis ofEscherichia coliby milk: IV. The bacteriostatic antibody of human milk

Antibacterial performance of bovine lactoferrin-fish gelatine electrospun membranes

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