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.read more
Citations
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Journal ArticleDOI
Constitutive expression of human lactoferrin and its N-lobe in rice plants to confer disease resistance.
Kenji Takase,Kiyoshi Hagiwara,Haruko Onodera,Yaeko Nishizawa,Masashi Ugaki,Toshihiro Omura,Shinichi Numata,Katsuki Akutsu,Haruto Kumura,Kei-ichi Shimazaki +9 more
TL;DR: Deglycosylation experiments suggested that both proteins produced by the plants had plant-type oligosaccharide chains, and significant resistance against Burkholderia (Pseudomonas) plantarii, the causative agent of bacterial seedling blight disease, was observed in the transgenic plants expressing HLF or HLFN.
Book ChapterDOI
Direct detection and quantitative determination of bovine lactoferricin and lactoferrin fragments in human gastric contents by affinity mass spectrometry.
TL;DR: Bovine Lfcin can be produced in the human stomach after ingestion of an infant formula supplemented with bovine lactoferrin, and this method developed a method of surface-enhanced laser desorption/ionization (SELDI) affinity mass spectrometry using n-butyl terminal groups for surface- enhanced affinity capture (SEAC) to quantify not only LFCin generated in vivo but also other lact oferrin fragments.
Journal ArticleDOI
Study of the interaction of lactoferricin B with phospholipid monolayers and bilayers.
TL;DR: The results obtained on monolayers are correlated by fluorescent probe release measurements of dye-containing vesicles made of lipids in different phases and support the important role of the lipid fluidity and packing on the activity of LfcinB.
Journal ArticleDOI
Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides.
Špela Gruden,Nataša Poklar Ulrih +1 more
TL;DR: In this article, the authors defined the current antibacterial, antiviral, antifungal, and antiparasitic activities of lactoferrins, lactoferricins, and lactof-derived peptides.
Journal ArticleDOI
Bactericidal activity of lactoferrin and its amidated and pepsin-digested derivatives against Pseudomonas fluorescens in ground beef and meat fractions.
TL;DR: EDTA at 5 mM greatly enhanced the bactericidal activity of the three antimicrobials at 1 mg/ml in meat homogenate and in the presence of 5 mM sodium bicarbonate, whereas the effectiveness of LF and PDLF remained 1.0 and 0.4 log units lower, respectively, than the results obtained in distilled water.
References
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Journal ArticleDOI
Identification of the bactericidal domain of lactoferrin.
Wayne Robert Bellamy,Mitsunori Takase,Koji Yamauchi,Hiroyuki Wakabayashi,Kouzou Kawase,Mamoru Tomita +5 more
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.
David Wade,Anita Boman,Birgitta Wahlin,Charles Michael Drain,David Andreu,Hans G. Boman,R. B. Merrifield +6 more
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.
Journal ArticleDOI
Cell-free immunity in insects.
Hans G. Boman,Dan Hultmark +1 more
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.
rd R T Ellison,T. J. Giehl +1 more
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.