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
Production of Recombinant Bovine Lactoferrin N-Lobe in Insect Cells and Its Antimicrobial Activity
Ichiro Nakamura,Atsushi Watanabe,Hiroshi Tsunemitsu,Nai-Yuan Lee,Haruto Kumura,Kei-ichi Shimazaki,Yukio Yagi +6 more
TL;DR: A gene encoding the N-terminal half (N-lobe) of bovine lactoferrin was cloned and expressed in cultured insect cells using a baculovirus expression system and showed no potency to inhibit the growth of bacteria.
Journal ArticleDOI
Synergistic antibacterial efficacies of the combination of bovine lactoferrin or its hydrolysate with probiotic secretion in curbing the growth of meticillin-resistant Staphylococcus aureus.
TL;DR: A combinatorial treatment approach by using the well-documented antibacterial protein apo-bovine lactoferrin or its hydrolysate and specific probiotic supernatants for controlling MRSA infection suggested that L. fermentum could be the best candidate to be used with apO-bLf or bLf-hydrolysate as a live supplement against MRSA infections.
Journal ArticleDOI
Structure of iron saturated C-lobe of bovine lactoferrin at pH 6.8 indicates a weakening of iron coordination
Nilisha Rastogi,Avinash Singh,Prashant Singh,Tapesh K. Tyagi,Sada N. Pandey,Kouichirou Shin,Punit Kaur,Sujata Sharma,Tej P. Singh +8 more
TL;DR: It may be stated that His595 is the first residue to dissociate from ferric ion when the pH is lowered, based on the present structure of iron saturated C‐lobe.
Book ChapterDOI
Glycation Ligand Binding Motif in Lactoferrin
TL;DR: The elevated AGEs may inhibit endogenous antibacterial proteins by binding to the conserved ABCD motif, thereby increasing susceptibility to bacterial infections in diabetic individuals and may provide a basis for the development of new approaches to prevent diabetic infections.
Journal ArticleDOI
Antibacterial activity of multiple antigen peptides homologous to a loop region in human lactoferrin
Masachika Azuma,T. Kojima,I. Yokoyama,Hisao Tajiri,Kazuhiro Yoshikawa,S Saga,C. A. Del Carpio +6 more
TL;DR: A novel possibility for MAP to increase the activity of antibiotic peptides other than simply to stimulate antibody production is shown, as reported so far.
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.