Increased<i>Staphylococcus</i>-killing Activity of an Antimicrobial Peptide, Lactoferricin B, with Minocycline and Monoacylglycerol

Wakabayashi, Hiroyuki; Teraguchi, Susumu; Tamura, Yoshitaka

doi:10.1271/bbb.66.2161

Cited by 19 publications

(14 citation statements)

References 25 publications

(17 reference statements)

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“…Thus, peptides potentiated the antibiotics tested-all of them substrates of the MexAB-OprM system, except the most hydrophilic ones, the beta-lactams cefotaxime and ticarcillin. It has been hypothesized that the ability of lactoferricin to counteract efflux pump activity is due not only to its membrane-disorganizing nature but also to dissipation of the proton-motive force, resulting in decreased activity of ATP-dependent multidrug efflux pumps (63). The latter activity has also been reported in peptides unrelated to lactoferricin (51).…”

Section: Discussionmentioning

confidence: 99%

Structural Features Governing the Activity of Lactoferricin-Derived Peptides That Act in Synergy with Antibiotics against Pseudomonas aeruginosa In Vitro and In Vivo

Sánchez-Gómez

Japelj

Jerala

et al. 2011

Antimicrob Agents Chemother

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Pseudomonas aeruginosa is naturally resistant to many antibiotics, and infections caused by this organism are a serious threat, especially to hospitalized patients. The intrinsic low permeability of P. aeruginosa to antibiotics results from the coordinated action of several mechanisms, such as the presence of restrictive porins and the expression of multidrug efflux pump systems. Our goal was to develop antimicrobial peptides with an improved bacterial membrane-permeabilizing ability, so that they enhance the antibacterial activity of antibiotics. We carried out a structure activity relationship analysis to investigate the parameters that govern the permeabilizing activity of short (8-to 12-amino-acid) lactoferricin-derived peptides. We used a new class of constitutional and sequence-dependent descriptors called PEDES (peptide descriptors from sequence) that allowed us to predict (Spearman's ‫؍‬ 0.74; P < 0.001) the permeabilizing activity of a new peptide generation. To study if peptide-mediated permeabilization could neutralize antibiotic resistance mechanisms, the most potent peptides were combined with antibiotics, and the antimicrobial activities of the combinations were determined on P. aeruginosa strains whose mechanisms of resistance to those antibiotics had been previously characterized. A subinhibitory concentration of compound P2-15 or P2-27 sensitized P. aeruginosa to most classes of antibiotics tested and counteracted several mechanisms of antibiotic resistance, including loss of the OprD porin and overexpression of several multidrug efflux pump systems. Using a mouse model of lethal infection, we demonstrated that whereas P2-15 and erythromycin were unable to protect mice when administered separately, concomitant administration of the compounds afforded long-lasting protection to one-third of the animals.

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Section: Discussionmentioning

confidence: 99%

Structural Features Governing the Activity of Lactoferricin-Derived Peptides That Act in Synergy with Antibiotics against Pseudomonas aeruginosa In Vitro and In Vivo

Sánchez-Gómez

Japelj

Jerala

et al. 2011

Antimicrob Agents Chemother

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“…Lfc has been reported to have high antimicrobial activity in vitro (Bellamy et al 1993;Shin et al 1998;Wakabayashi et al 2002). Zhang et al (1998) found that Lfc antibacterial activity is higher than that of shiva-1, which is one of the most widely reported bactericidal peptides.…”

Section: Discussionmentioning

confidence: 99%

“…Lfc has stronger antimicrobial activity against various human pathogenic bacteria (Aguilera et al 1999;Bellamy et al 1992b;Sánchez-Gómez et al 2008;Shin et al 1998;Wakabayashi et al 2002), fungi (Bellamy et al 1993), and viruses (Marr et al 2009) compared to that of lactoferrin. e antimicrobial activity of Lfc against plant pathogenic bacteria (Zhang et al 1998) and fungi (Muños and Marcos 2006) has also been studied.…”

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confidence: 99%

Transgenic tobacco plants expressing antimicrobial peptide bovine lactoferricin show enhanced resistance to phytopathogens

Fukuta

Kawamoto²,

Mizukami

et al. 2012

Plant Biotechnology

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Lactoferricin B, the antimicrobially active N-terminal peptide derived from acid pepsin hydrolysis of bovine lactoferrin, has broad spectrum antimicrobial activities. We expressed the lactoferricin gene in tobacco plants to evaluate its antimicrobial activity. e coding region for the chimeric peptide gene of the signal peptide from tobacco pathogenrelated protein (PR-1) and bovine lactoferricin was synthesized using the recombinant polymerase chain reaction (PCR) method. Transgenic tobacco plants expressing the lactoferricin gene were developed using the Agrobacterium-mediated transformation method. e lactoferricin B gene was integrated into the tobacco genome and its transcription was detected by PCR, Southern blot analysis, and reverse transcription PCR (RT-PCR), respectively. e transgenic tobacco plants were challenged with the pathogenic bacteria Pseudomonas syringae pv. tabaci and Botrytis cinerea. At 30 or 28 days postinoculation, the transgenic plants were still green and continued to grow, whereas the control plants were infected with bacterial or fungal pathogens from the roots to the tips, resulting in death of the plants. In conclusion, transgenic tobacco plants that overexpressed the lactoferricin gene, linked to the signal peptide of tobacco PR-1 protein under the control of a high expression constitutive promoter, showed enhanced resistance to bacterial (P. syringae pv. tabaci) and fungal (B. cinerea) diseases.

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“…Wakabayashi investigated the effects of bLfcin combined with antibiotics or various other compounds against S. aureus [88].…”

Section: Synergy With Antibacterial and Anti-fungal Drugsmentioning

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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IncreasedStaphylococcus-killing Activity of an Antimicrobial Peptide, Lactoferricin B, with Minocycline and Monoacylglycerol

Cited by 19 publications

References 25 publications

Structural Features Governing the Activity of Lactoferricin-Derived Peptides That Act in Synergy with Antibiotics against Pseudomonas aeruginosa In Vitro and In Vivo

Structural Features Governing the Activity of Lactoferricin-Derived Peptides That Act in Synergy with Antibiotics against Pseudomonas aeruginosa In Vitro and In Vivo

Transgenic tobacco plants expressing antimicrobial peptide bovine lactoferricin show enhanced resistance to phytopathogens

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

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