Ultrastructural effects of antimicrobial peptides from bovine lactoferrin on the membranes of Candida albicans and Escherichia coli

Kraan, Marieke I.A. van der; Marle, J. van; Nazmi, Kamran; Groenink, J.; Hof, Wim van ’t; Veerman, E.C.I.; Bolscher, Jan G. M.; Amerongen, A. van Nieuw

doi:10.1016/j.peptides.2005.02.011

Cited by 67 publications

(46 citation statements)

References 24 publications

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“…All cultures were stored in skim milk (Difco, Detroit, MI, USA) at À20 C. Working cultures were obtained by transferring a loop of the stock culture into 10 ml of tryptic soy broth (TSB; Merck, Darmstadt, Alemania), incubating overnight and transferring a loop to tryptic soy agar (TSA; Merck, Darmstadt, Alemania). After an overnight incubation, an isolated colony was transferred to 10 ml of TSB and then incubated at 37 C for 16-20 h.…”

Section: Methodsmentioning

confidence: 99%

“…Porcine pepsin (Sigma, Poole, UK) was added to achieve a final concentration of 3% (w/w of the substrate). The mixture was incubated at 37 C for 4 h, and the hydrolysis reaction was stopped by heating at 80 C for 15 min. The pH value of the solution was adjusted to 7, and the insoluble peptides formed were removed by centrifugation at 15;000 Â g for 15 min.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Antibacterial Activity of Recombinant Human Lactoferrin from Rice: Effect of Heat Treatment

Conesa

Rota

Castillo

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Antibacterial Activity of Recombinant Human Lactoferrin from Rice: Effect of Heat Treatment

Conesa

Rota

Castillo

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…membrane within the range 18 to 60 µg/mL (MIC). Cells of nine different strains exposed to bLfcin exhibited severe ultra-structural damage, reflecting the peptide's induction of an autolytic response [83].…”

Section: In Vitro Antibacterial and Anti-fungal Activitymentioning

confidence: 99%

Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine

Bruni¹,

et al. 2016

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Antimicrobial peptides (AMPs) represent a vast array of molecules produced by virtually all living organisms as natural barriers against infection. Among AMP sources, an interesting class regards the food-derived bioactive agents. The whey protein lactoferrin (Lf) is an iron-binding glycoprotein that plays a significant role in the innate immune system, and is considered as an important host defense molecule. In search for novel antimicrobial agents, Lf offers a new source with potential pharmaceutical applications. The Lf-derived peptides Lf(1-11), lactoferricin (Lfcin) and lactoferrampin exhibit interesting and more potent antimicrobial actions than intact protein.Particularly, Lfcin has demonstrated strong antibacterial, anti-fungal and antiparasitic activity with promising applications both in human and veterinary diseases (from ocular infections to osteo-articular, gastrointestinal and dermatological diseases).

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“…In E. coli, depolarization and large effects on the integrity of cytoplasmic membrane have been shown. 6,7 Lf and Lfcin B have been shown to be effective synergistic agents when used in combination with antibiotics. 6 Among Gram-negative bacteria, Lf enhances the sensitivity of Pseudomonas aeruginosa to chloramphenicol, 8 of Stenotrophomonas maltophilia to rifampin, 9 of Salmonella enterica to erythromycin 10 and of E. coli to novobiocin.…”

mentioning

confidence: 99%

“…The overall results achieved on interaction between Lfcin B and fluoroquinolones in both E. coli-susceptible and -resistant strains are possibly due to the membrane-disorganizing nature of this peptide, 6,7 which leads not only to increased permeability through the bacterial cell wall but also to the dissipation of the proton-motive force, resulting in decreased activity of ATP-dependent multi-drug efflux pumps. 6 At sub-inhibiting concentrations, Lfcin B may affect the access/efflux of drugs, thus modifying the quinolone concentrations required to inhibit growth.…”

mentioning

confidence: 99%

Effect of lactoferricin on fluoroquinolone susceptibility of uropathogenic Escherichia coli

et al. 2009

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Members of the Enterobacteriaceae family are mainly involved in the etiology of urinary tract infections, and Escherichia coli is by far the most common microorganism isolated from about 50% of all nosocomial and 90% of outpatients' urinary tract infections. 1 Quinolones are effective antibacterial agents that are commonly used as antimicrobials in the management of urinary tract infections, owing to which the rates of antimicrobial resistance among E. coli strains have increased greatly during the past two decades. 1,2 Bacteria are able to develop resistance by point mutations in chromosomal genes codifying DNA gyrase and topoisomerase IV targeted by quinolones. 3 Other mechanisms involve mutations affecting the accumulation of fluoroquinolones in the bacterial cell, such as the expression of outer membrane proteins and alteration in the lipopolysaccharide. 3 Furthermore, plasmid-mediated resistance has also been identified: qnr gene products capable of protecting DNA gyrase and AAC(6¢)-Ib-cr, a variant aminoglycoside acetyltransferase, providing enzymatic antibiotic inactivation. 3 The emergence of bacterial strains exhibiting resistance against conventional antibiotics has encouraged the search for novel antimicrobial strategies. Among the compounds that are currently under investigation for their therapeutic potential are a number of antimicrobial peptides. 4 The positively charged antimicrobial peptide lactoferricin B (Lfcin B), a 25-amino-acid peptide released from the N-terminal part of bovine lactoferrin (Lf) by gastric pepsin cleavage, has recently received attention due to its broad host defense properties against bacteria, fungi and parasites. 5,6 Lfcin B is active toward Gram-positive and Gram-negative species, including E. coli. This peptide contains many hydrophobic and positively charged residues, which enable its interaction with negatively charged biological membranes. In E. coli, depolarization and large effects on the integrity of cytoplasmic membrane have been shown. 6,7 Lf and Lfcin B have been shown to be effective synergistic agents when used in combination with antibiotics. 6 Among Gram-negative bacteria, Lf enhances the sensitivity of Pseudomonas aeruginosa to chloramphenicol, 8 of Stenotrophomonas maltophilia to rifampin, 9 of Salmonella enterica to erythromycin 10 and of E. coli to novobiocin. 11 Lfcin B has been shown to act synergistically with erythromycin, 12 and a synergistic growth-inhibitory activity by bovine Lf lysate and gentamicin toward E. coli was observed. 13 In this study, we primarily analyzed the susceptibility of uropathogenic E. coli strains to fluoroquinolones. As E. coli fluoroquinolone resistance has been associated with reductions in virulence traits and shifts from the phylogenetic group B2 toward groups A, B1 or D, 2 we then compared antibiotic resistance with the strains belonging to phylogenetic groups and with the occurrence of some capsular determinants that can be considered as cell protection genes. In succession, to gain insight into the interference of...

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Ultrastructural effects of antimicrobial peptides from bovine lactoferrin on the membranes of Candida albicans and Escherichia coli

Cited by 67 publications

References 24 publications

Antibacterial Activity of Recombinant Human Lactoferrin from Rice: Effect of Heat Treatment

Antibacterial Activity of Recombinant Human Lactoferrin from Rice: Effect of Heat Treatment

Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine

Effect of lactoferricin on fluoroquinolone susceptibility of uropathogenic Escherichia coli

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