Ultrastructural effects and antibiofilm activity of LFchimera against Burkholderia pseudomallei

Puknun, Aekkalak; Kanthawong, Sakawrat; Anutrakunchai, Chitchanok; Nazmi, Kamran; Tigchelaar, Wikky; Hoeben, Kees A.; Veerman, E.C.I.; Bolscher, Jan G. M.; Taweechaisupapong, Suwimol

doi:10.1007/s11274-015-1988-x

Cited by 11 publications

(9 citation statements)

References 43 publications

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“…The greater antimicrobial efficacy exhibited by LFchimera compared to its peptides of origin, LFcin17-30 and LFampin265-284 has been observed in other studies, including studies testing the antibacterial effects of these peptides against pathogenic microorganisms, such as Candida, the halophiles V.parahaemolyticus and V. cholera, S. aureus, E. histolytica and E. coli (Bolscher et al 2012; Flores-Villasenor et al 2012a;Soto et al 2010;Puknun et al 2016). LFchimera has also been reported to exert antimicrobial activity against Burkholderia pseudomallei, Burkholderia thailandensis and Leishmania donovani…”

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confidence: 76%

“…The peptides magainin II and amikacin had no effect on EAEC viability at the concentrations and conditions used here (data not shown). (Puknun et al 2013;Puknun et al 2016;Silva et al 2012;Silva et al 2013). The high antimicrobial activity of LFchimera may be related to its structure, which adopts a secondary conformation (three-dimensional) that resembles that of native bLF (Bolscher et al 2009).…”

Section: Electron Microscopymentioning

confidence: 99%

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Antibacterial and cell penetrating effects of LFcin17–30, LFampin265–284, and LF chimera on enteroaggregative Escherichia coli

Reyes-Cortés

Acosta-Smith

Mondragón-Flores

et al. 2017

Biochem. Cell Biol.

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Lactoferrin (LF) is a protein with antimicrobial activity, which is conferred in part by 2 regions contained in its N-terminal lobe. These regions have been used to develop the following synthetic peptides: lactoferricin17–30, lactoferrampin265–284, and LF chimera (a fusion of lactoferricin17–30 and lactoferrampin265–284). We have reported that these LF peptides have antibacterial activity against several pathogenic bacteria; however, the exact mechanism of action has not been established. Here, we report the effects of LF peptides on the viability of enteroaggregative Escherichia coli (EAEC) and the ability of these peptides to penetrate into the bacteria cytoplasm. The viability of EAEC treated with LF peptides was determined via enumeration of colony-forming units, and the binding and internalization of the LF peptides was followed via immunogold labeling and electron microscopy. Treatment of EAEC with 20 and 40 μmol/L LF peptides reduced bacterial growth compared with untreated bacteria. Initially the peptides associated with the plasma membrane, but after 5 to 30 min of incubation, the peptides were found in the cytoplasm. Remarkably, bacteria treated with LF chimera developed cytosolic electron-dense structures that contained the antimicrobial peptide. Our results suggest that the antibacterial mechanism of LF peptides on EAEC involves their interaction with and penetration into the bacteria.

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confidence: 76%

Section: Electron Microscopymentioning

confidence: 99%

Antibacterial and cell penetrating effects of LFcin17–30, LFampin265–284, and LF chimera on enteroaggregative Escherichia coli

Reyes-Cortés

Acosta-Smith

Mondragón-Flores

et al. 2017

Biochem. Cell Biol.

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“…For example, recently the antimicrobial activities of the LFchimera were tested against isolates of Burkholderia pseudomallei and compared to the preferential antibiotic of use ceftazidime (CAZ). All isolates including B. pseudomallei 979b shown to be resistant to CAZ, could be killed by 5–10 μM of LFchimera within 2 h, while CAZ, and LFcin17–30 and LFampin265–284 individually only inhibited the B. pseudomallei strains, still resulting in an overgrowth in 24 h (Puknun et al 2016). …”

Section: Discussionmentioning

confidence: 99%

“…The potency of this chimeric peptide provoked us to test the peptide against various human pathogens, like Staphylococcus aureus (Flores-Villasenor et al 2010) Escherichia coli O157:H7 (Flores-Villasenor et al 2012), Streptococcus pneumoniae Leon-Sicairos et al 2014) and Burkholderia pseudomallei (Kanthawong et al 2009; Puknun et al 2013, 2016), the latter which is classified by the Centers for Disease Control and Prevention as a category B biological warfare agent (BWA) (Rotz et al 2002). …”

Section: Introductionmentioning

confidence: 99%

Effects of lactoferrin derived peptides on simulants of biological warfare agents

Sijbrandij

Ligtenberg

Nazmi

et al. 2016

World J Microbiol Biotechnol

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Lactoferrin (LF) is an important immune protein in neutrophils and secretory fluids of mammals. Bovine LF (bLF) harbours two antimicrobial stretches, lactoferricin and lactoferampin, situated in close proximity in the N1 domain. To mimic these antimicrobial domain parts a chimeric peptide (LFchimera) has been constructed comprising parts of both stretches (LFcin17–30 and LFampin265–284). To investigate the potency of this construct to combat a set of Gram positive and Gram negative bacteria which are regarded as simulants for biological warfare agents, the effect on bacterial killing, membrane permeability and membrane polarity were determined in comparison to the constituent peptides and the native bLF. Furthermore we aimed to increase the antimicrobial potency of the bLF derived peptides by cationic amino acid substitutions. Overall, the bactericidal activity of the peptides could be related to membrane disturbing effects, i.e. membrane permeabilization and depolarization. Those effects were most prominent for the LFchimera. Arginine residues were found to be crucial for displaying antimicrobial activity, as lysine to arginine substitutions resulted in an increased antimicrobial activity, affecting mostly LFampin265–284 whereas arginine to lysine substitutions resulted in a decreased bactericidal activity, predominantly in case of LFcin17–30.

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“…The bactericidal activity of LFchimera has been definitively stronger than that of the peptides (LFcin17-30 and LFampin265-284), as has been demonstrated in many experiments; due to lower concentrations, shorter incubation time, and salt concentrations present in the environment (needed for the growth of halophile bacteria) permit the bactericidal activity of LF chimera, compared with the peptides that conform this molecule which is not effective at these conditions (Bolscher et al, 2009 ; Haney et al, 2009 ; Leon-Sicairos et al, 2014 ). Otherwise, the microbicidal effect of LFchimera against Candida spp, Vibrio parahaemolyticus, Staphylococcus aureus , enterotoxigenic and enterohaemorragic Escherichia coli , or in the parasites Entamoeba histolytica, Burkholderia thailandensis , and Leishmania pifanoi has been established in vitro (Bolscher et al, 2009 ; Lopez-Soto et al, 2009 , 2010 ; Flores-Villasenor et al, 2010 , 2012 ; Kanthawong et al, 2014 ; Leon-Sicairos et al, 2014 ; Puknun et al, 2016 ).…”

Section: Introductionmentioning

confidence: 99%

Bovine Lactoferrin and Lactoferrin-Derived Peptides Inhibit the Growth of Vibrio cholerae and Other Vibrio species

et al. 2018

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Vibrio is a genus of Gram-negative bacteria, some of which can cause serious infectious diseases. Vibrio infections are associated with the consumption of contaminated food and classified in Vibrio cholera infections and non-cholera Vibrio infections. In the present study, we investigate whether bovine lactoferrin (bLF) and several synthetic peptides corresponding to bLF sequences, are able to inhibit the growth or have bactericidal effect against V. cholerae and other Vibrio species. The antibacterial activity of LF and LF-peptides was assessed by kinetics of growth or determination of colony forming unit in bacteria treated with the peptides and antibiotics. To get insight in the mode of action, the interaction between bLF and bLF-peptides (coupled to FITC) and V. cholera was evaluated. The damage of effector-induced bacterial membrane permeability was measured by inclusion of the fluorescent dye propidium iodide using flow cytometry, whereas the bacterial ultrastructural damage in bacteria treated was observed by transmission electron microscopy. The results showed that bLF and LFchimera inhibited the growth of the V. cholerae strains; LFchimera permeabilized the bacteria which membranes were seriously damaged. Assays with a multidrug-resistant strain of Vibrio species indicated that combination of sub-lethal doses of LFchimera with ampicillin or tetracycline strongly reduced the concentration of the antibiotics to reach 95% growth inhibition. Furthermore, LFchimera were effective to inhibit the V. cholerae counts and damage due to this bacterium in a model mice. These data suggest that LFchimera and bLF are potential candidates to combat the V. cholerae and other multidrug resistant Vibrio species.

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Ultrastructural effects and antibiofilm activity of LFchimera against Burkholderia pseudomallei

Cited by 11 publications

References 43 publications

Antibacterial and cell penetrating effects of LFcin17–30, LFampin265–284, and LF chimera on enteroaggregative Escherichia coli

Antibacterial and cell penetrating effects of LFcin17–30, LFampin265–284, and LF chimera on enteroaggregative Escherichia coli

Effects of lactoferrin derived peptides on simulants of biological warfare agents

Bovine Lactoferrin and Lactoferrin-Derived Peptides Inhibit the Growth of Vibrio cholerae and Other Vibrio species

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