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Journal ArticleDOI

Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin

TLDR
Lactoferricin B was lethal, causing a rapid loss of colony-forming capability in most of the species tested, and Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.
Abstract
A physiologically diverse range of Gram-positive and Gram-negative bacteria was found to be susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by gastric pepsin digestion of bovine lactoferrin. The list of susceptible organisms includes Escherichia coli, Salmonella enteritidis, Klebsiella pneumoniae, Proteus vulgaris, Yersinia enterocolitica, Pseudomonas aeruginosa, Campylobacter jejuni, Staphylococcus aureus, Streptococcus mutans, Corynebacterium diphtheriae, Listeria monocytogenes and Clostridium perfringens. Concentrations of lactoferricin B required to cause complete inhibition of growth varied within the range of 0.3 to 150 micrograms/ml, depending on the strain and the culture medium used. The peptide showed activity against E. coli O111 over the range of pH 5.5 to 7.5 and was most effective under slightly alkaline conditions. Its antibacterial effectiveness was reduced in the presence of Na+, K+, Mg2+ or Ca2+ ions, or in the presence of various buffer salts. Lactoferricin B was lethal, causing a rapid loss of colony-forming capability in most of the species tested. Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.

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Citations
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Journal ArticleDOI

Latent bioactive peptides in milk proteins: proteolytic activation and significance in dairy processing.

TL;DR: The ability of proteolytic enzymes from various sources, especially from lactic acid bacteria, to release bioactive peptides and the physiological and biotechnological significance of these peptides in dairy products are reviewed.
Journal ArticleDOI

Whey components: millennia of evolution create functionalities for mammalian nutrition: what we know and what we may be overlooking.

TL;DR: Food and nutrition research must move beyond the description of food ingredients as delivering only essential nutrients and develop a mechanistic understanding of the interactions between dietary components and the metabolic and physiological properties of the intestine.
Journal ArticleDOI

Lactoferrin and host defense.

TL;DR: It is suggested that lactoferrin functions as a key component of mammalian host defense at the mucosal surface in mice and humans.
Journal ArticleDOI

The non-enzymatic microbicidal activity of lysozymes.

TL;DR: It is demonstrated here that amphipathic helix stretches in the C‐terminus of T4 lysozyme mediate its bactericidal and fungistatic activities and opens up many new opportunities for optimization of lysozymes as antimicrobial agents in various applications by protein engineering.
Journal ArticleDOI

Antiviral properties of lactoferrin--a natural immunity molecule.

TL;DR: The capability of lactoferrin to exert a potent antiviral activity, through its binding to host cells and/or viral particles, and its nuclear localization strengthens the idea that lact oferrin is an important brick in the mucosal wall, effective against viral attacks and it could be usefully applied as novel strategy for treatment of viral infections.
References
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Journal ArticleDOI

Identification of the bactericidal domain of lactoferrin.

TL;DR: The studies suggest this domain is the structural region responsible for the bacterial properties of lactoferrin, having effectiveness against various Gram-negative and Gram-positive bacteria at concentrations between 0.3 microM and 3.0 microM, depending on the target strain.
Journal ArticleDOI

All-D amino acid-containing channel-forming antibiotic peptides.

TL;DR: The D enantiomers of three naturally occurring antibiotics--cecropin A, magainin 2 amide, and melittin--were synthesized and it is suggested that the mode of action of these peptides on the membranes of bacteria, erythrocytes, plasmodia, and artificial lipid bilayers may be similar and involves the formation of ion-channel pores spanning the membranes, but without specific interaction with chiral receptors or enzymes.
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Cell-free immunity in insects.

TL;DR: The authors showed that at least two of the cecropins originate from a gene duplication and that the biosynthesis has been initiated on RNA and tissue levels on both RNA and DNA levels.
Journal ArticleDOI

Killing of gram-negative bacteria by lactoferrin and lysozyme.

TL;DR: Dialysis chamber studies indicate that bacterial killing requires direct contact with lactoferrin, and work with purified LPS suggests that this relates to direct LPS-binding by the protein, suggesting that their interaction contributes to host defense.
Journal ArticleDOI

A bactericidal effect for human lactoferrin

TL;DR: Streptococcus mutans and Vibrio cholerae, but not Escherichia coli, were killed by incubation with purified human apolact oferrin, contingent upon the metal-chelating properties of the lactoferrin molecule.
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