The Antibacterial Activity of Lactoferrin and Neonatal E. coli Infections

Reiter, B.; Perraudin, J. P.

doi:10.1007/978-1-4757-9068-9_21

Cited by 13 publications

(10 citation statements)

References 10 publications

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“…In several Gram-negative bacteria, lactoferrin damages their outer membranes and releases LPS from the cells (40). In P. gingivalis, no significant release of LPS, fimbriae/fimbrillin, or the HA proteins was found after lactoferrin treatment.…”

Section: Discussionmentioning

confidence: 94%

Human Lactoferrin Binds and Removes the Hemoglobin Receptor Protein of the Periodontopathogen Porphyromonas gingivalis

Shi

Kong

Nakayama

2000

Journal of Biological Chemistry

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Porphyromonas gingivalis possesses a hemoglobin receptor (HbR) protein on the cell surface as one of the major components of the hemoglobin utilization system in this periodontopathogenic bacterium. HbR is intragenically encoded by the genes of an arginine-specific cysteine proteinase (rgpA), lysine-specific cysteine proteinase (kgp), and a hemagglutinin (hagA). Here, we have demonstrated that human lactoferrin as well as hemoglobin have the abilities to bind purified HbR and the cell surface of P. gingivalis through HbR. The interaction of lactoferrin with HbR led to the release of HbR from the cell surface of P. gingivalis. This lactoferrinmediated HbR release was inhibited by the cysteine proteinase inhibitors effective to the cysteine proteinases of P. gingivalis. P. gingivalis could not utilize lactoferrin for its growth as an iron source and, in contrast, lactoferrin inhibited the growth of the bacterium in a rich medium containing hemoglobin as the sole iron source. Lactoferricin B, a 25-amino acid-long peptide located at the N-lobe of bovine lactoferrin, caused the same effects on P. gingivalis cells as human lactoferrin, indicating that the effects of lactoferrin might be attributable to the lactoferricin region. These results suggest that lactoferrin has a bacteriostatic action on P. gingivalis by binding HbR, removing it from the cell surface, and consequently disrupting the iron uptake system from hemoglobin.

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Section: Discussionmentioning

confidence: 94%

Human Lactoferrin Binds and Removes the Hemoglobin Receptor Protein of the Periodontopathogen Porphyromonas gingivalis

Shi

Kong

Nakayama

2000

Journal of Biological Chemistry

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“…A variety of anti‐microbial activity of Lf is reported, such as bacteriostatic (Ogata et al., 1988), anti‐bacterial (Reiter and Perraudin, 1998), anti‐candidial (van den Berg et al., 2000) and anti‐viral (Ikeda et al., 2000) actions. The intestine of herbivores is also exposed to a variety of pathogens from their feed stuffs.…”

Section: Discussionmentioning

confidence: 99%

Characteristics of Lactoferrin Receptor in Bovine Intestine: Higher Binding Activity to the Epithelium Overlying Peyer's Patches

Talukder

Takeuchi

Harada

2003

Journal of Veterinary Medicine Series A

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Several lines of evidence have recently demonstrated the occurrence of specific lactoferrin (Lf) receptors in different cells. We report here, for the first time, the characteristics of binding, and distribution of Lf receptors in the bovine intestinal tract with special emphasis on the epithelium overlying Peyer's patches (EOPP). Brush-border membrane vesicles (BBMV) were prepared from the mucosa of duodenum, jejunum, ileum, colon, EOPP in jejunum and EOPP in ileum. Receptor binding assays were carried out using 125I-labelled bovine Lf. Specific and saturable Lf receptors were found in BBMV of all the intestinal segments examined. Non-linear regression and Scatchard plot analyses clearly revealed that EOPP had the highest binding maximal (Bmax), and lowest in colon. The maximum dissociation constant (Kd) 3.74 microm was in the ileum. We found that bovine transferrin competed with Lf for the same binding site of receptors. In contrast, no binding of bovine serum albumin occurred. It was concluded that Lf receptors in the mucosal lining are attributable to mediate multifunctional activities of Lf in the gut, especially in the EOPP.

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“…Lactoferrin can deprive the bacteria or fungus of this essential nutrient for growth. [15][16][17][18] The action of lactoferrin depends on an iron-poor environment. Saturation of lactoferrin with endogenous iron abolishes this activity.…”

Section: Discussionmentioning

confidence: 99%

Effects of Powdered Human Milk Fortifiers on the Antibacterial Actions of Human Milk

Chan

2003

J Perinatol

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The Antibacterial Activity of Lactoferrin and Neonatal E. coli Infections

Cited by 13 publications

References 10 publications

Human Lactoferrin Binds and Removes the Hemoglobin Receptor Protein of the Periodontopathogen Porphyromonas gingivalis

Human Lactoferrin Binds and Removes the Hemoglobin Receptor Protein of the Periodontopathogen Porphyromonas gingivalis

Characteristics of Lactoferrin Receptor in Bovine Intestine: Higher Binding Activity to the Epithelium Overlying Peyer's Patches

Effects of Powdered Human Milk Fortifiers on the Antibacterial Actions of Human Milk

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