The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm

Haukland, Hanne H.; Ulvatne, Hilde; Sandvik, Kjersti; Vorland, Lars H.

doi:10.1016/s0014-5793(01)03100-3

Cited by 120 publications

(85 citation statements)

References 25 publications

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“…The mechanism by which Cecropin P1 disrupts the cell membrane of bacteria has been fully characterized. In contrast, Haukland et al (20) have proved that Lfcin B can penetrate the cell membrane without disruption; yet, Cecropin P1 has only been found to surround the membrane.…”

Section: Resultsmentioning

confidence: 93%

“…Some AMPs have been proven to penetrate the cell membrane and affect the intracellular targets within the cells (11)(12)(13); Lfcin B is one of these AMPs (14 -18). Some studies have indicated that Lfcin B leads to the depolarization of the cell membrane and does not lyse the cells (19); Lfcin B has been shown to inhibit the macromolecular synthesis of cells, which suggests that the intracellular targets of Lfcin B may exist (12,19,20).…”

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confidence: 99%

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Lactoferricin B Inhibits the Phosphorylation of the Two-Component System Response Regulators BasR and CreB

Sung

Chen

2012

Molecular & Cellular Proteomics

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Natural antimicrobial peptides provide fundamental protection for multicellular organisms from microbes, such as Lactoferricin B (Lfcin B). Many studies have shown that Lfcin B penetrates the cell membrane and has intracellular activities. To elucidate the intracellular behavior of Lfcin B, we first used Escherichia coli K12 proteome chips to identify the intracellular targets of Lfcin B. The results showed that Lfcin B binds to two response regulators, BasR and CreB, of the two-component system. For further analysis, we conducted several in vitro and in vivo experiments and utilized bioinformatics methods. The electrophoretic mobility shift assays and kinase assays indicate that Lfcin B inhibits the phosphorylation of the response regulators (BasR and CreB) and their cognate sensor kinases (BasS and CreC). Antibacterial assays showed that Lfcin B reduced E. coli's tolerance to environmental stimuli, such as excessive ferric ions and minimal medium conditions. This is the first study to show that an antimicrobial peptide inhibits the growth of bacteria by influencing

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Section: Resultsmentioning

confidence: 93%

mentioning

confidence: 99%

Lactoferricin B Inhibits the Phosphorylation of the Two-Component System Response Regulators BasR and CreB

Sung

Chen

2012

Molecular & Cellular Proteomics

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“…AMPs comprise part of the innate immune system of many organisms and help protect the host species from microbial invasion/infection. Current dogma dictates that the antimicrobial activity of these peptides is mediated through interaction of AMPs with target cell membranes and subsequent membrane disruption, although other mechanisms have been postulated [12][13][14]. The current study expands on previous work developing AMP-based detection assays for Escherichia coli and Salmonella typhimurium [15,16].…”

Section: Introductionmentioning

confidence: 77%

Antimicrobial peptides as new recognition molecules for screening challenging species

Kulagina

Shaffer

Ligler

et al. 2007

Sensors and Actuators B: Chemical

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The goal of this study was to evaluate binding of four targets of biodefense interest to immobilized antimicrobial peptides (AMPs) in biosensor assays. Polymyxins B and E, melittin, cecropins A, B, and P, parasin, bactenecin and magainin-1, as well as control antibodies, were used as capture molecules for detection of Cy3-labeled Venezuelan equine encephalitis virus (VEE), vaccinia virus, C. burnetti and B. melitensis. Although VEE, vaccinia virus and C. burnetti did not show any binding activity to their corresponding capture antibodies, B. melitensis bound to immobilized antiBrucella monoclonal antibodies. The majority of the immobilized AMPs included in this study bound labeled VEE, vaccinia virus and C. burnetti in a concentration-dependent manner, and B. melitensis bound to polymyxin B, polymyxin E, and bactenecin. No binding was observed on immobilized magainin-1. In contrast to all bacterial targets tested to date, VEE and vaccinia virus demonstrated similar patterns of binding to all peptides. While the direct assay is generally replaced by a sandwich assay for analysis of real-world samples, direct binding experiments are commonly used to characterize specificity and sensitivity of binding molecules. In this case, they clearly demonstrate the capability of AMPs as recognition molecules for four biothreat agents.

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“…In general, AMPs are cationic, often amphipathic, which primarily kill bacteria by interacting and disrupting their cell membrane [10][11][12][13] . In a previous study, we introduced the 1-11 antimicrobial sequence of the human lactoferrin protein (hLf), the hLf1-11 peptide, as a potent AMP with capacity to reduce bacterial adhesion on titanium implants 8 .…”

Section: Introductionmentioning

confidence: 99%

Antibacterial Properties of hLf1–11 Peptide onto Titanium Surfaces: A Comparison Study Between Silanization and Surface Initiated Polymerization

et al. 2015

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Dental implant failure can be associated to infections which develop into periimplantitis. In order to reduce biofilm formation, several strategies focusing on the use of antimicrobial peptides (AMP) have been studied. To covalently immobilize these molecules onto metallic substrates several techniques have been developed, including silanization and polymer brush prepared by surface-initiated atom transfer radical polymerization (ATRP), with varied peptide binding yield and antibacterial performance. The aim of the present study was to compare the efficiency of these methods to immobilize the lactoferrin-derived hLf1-11 antibacterial peptide onto titanium, and evaluate their antibacterial activity in vitro.Smooth titanium samples were coated with hLf1-11 peptide under three different conditions: silanization with APTES, and polymer brush based coatings with two different silanes. Peptide presence was determined by X-ray photoelectron spectroscopy and the mechanical stability of the coatings was studied under ultrasonication. The LDH assays confirmed that HFFs viability and proliferation were no affected by the treatments. The in vitro antibacterial properties of the modified surfaces were tested with two oral strains (Streptococcus sanguinis and Lactobacillus salivarius) showing an outstanding reduction. A higher decrease in bacterial attachment was noticed when samples were modified by ATRP methods compared to silanization. This effect is likely due to the capacity to immobilize more peptide on the surfaces using polymer brushes and the non-fouling nature of polymer PDMA segment.3

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The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm

Cited by 120 publications

References 25 publications

Lactoferricin B Inhibits the Phosphorylation of the Two-Component System Response Regulators BasR and CreB

Lactoferricin B Inhibits the Phosphorylation of the Two-Component System Response Regulators BasR and CreB

Antimicrobial peptides as new recognition molecules for screening challenging species

Antibacterial Properties of hLf1–11 Peptide onto Titanium Surfaces: A Comparison Study Between Silanization and Surface Initiated Polymerization

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