Selectivity for and destruction of Salmonella typhimurium via a membrane damage mechanism of a cell-penetrating peptide ppTG20 analogue

Li, Lirong; Shi, Yonghui; Su, GuanFang; Li, Guowei

doi:10.1016/j.ijantimicag.2012.05.026

Cited by 49 publications

(35 citation statements)

References 30 publications

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“…7, A and B). These results are in agreement with recent reports showing that some CPPs may switch from penetrating mammalian cells with no apparent toxicity to peptides capable of killing/swelling bacterial cells (12,13). Understanding the mechanism involved in this functional switch may assist in designing CPPs.…”

Section: Discussionsupporting

confidence: 92%

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Cell Penetrating Peptides and Cationic Antibacterial Peptides

Plaza

Morales‐Nava

Diener

et al. 2014

Journal of Biological Chemistry

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Background: Iztli peptides (IP) are a new class of antibacterial peptides that could be internalized by receptor-mediated endocytosis in yeast. Results: IP-1 penetrates cells independently of endocytosis and makes pores in membranes with large electric potential. Conclusion: Antibacterial peptides like IP-1 make pores or penetrate membranes depending on the membrane potential. Significance: Antibacterial peptides with penetrating activity are robust to control bacterial infections.

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Section: Discussionsupporting

confidence: 92%

“…If so, CPPs may work as CAPs in the presence of bacterial cells. In agreement with this idea, several CPPs have been shown to have antibacterial activity (12,13). Furthermore, given that CPPs and CAPs act on cellular membranes, it can be assumed that these membranes modulate their functions.…”

Section: Cell Penetrating Peptides (Cpp) and Cationic Antibacterial Pmentioning

confidence: 77%

Cell Penetrating Peptides and Cationic Antibacterial Peptides

Plaza

Morales‐Nava

Diener

et al. 2014

Journal of Biological Chemistry

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“…The effects of Lfcin4 and Lfcin5 on the outer membrane of S. aureus ATCC25923 and S. enteritidis CVCC3377 were determined by measuring the uptake of NPN4445. Mid-log phase cells were washed with sterile normal saline three times and suspended in 5 mM HEPES buffer (pH 7.2, containing 5 mM glucose) to an OD at 600 nm of 0.5.…”

Section: Methodsmentioning

confidence: 99%

Killing of Staphylococcus aureus and Salmonella enteritidis and neutralization of lipopolysaccharide by 17-residue bovine lactoferricins: improved activity of Trp/Ala-containing molecules

Hao

Yang

Wang

et al. 2017

Sci Rep

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Bovine lactoferricin (LfcinB) has potent antibacterial, antifungal and antiparasitic activities but is also hemolytic. Our objective was to identify LfcinB17-31 derivatives with reduced hemolysis and improved antimicrobial activity via substituting Cys3, Arg4, Gln7, Met10, and Gly14 with more hydrophobic residues. Two peptides, Lfcin4 and Lfcin5, showed higher activity against Staphylococcus aureus and Salmonella enteritidis and lower hemolytic activity than the parent peptide LfcinB17-31. These peptides permeabilized the outer and inner membranes of S. enteritidis; however, Lfcin5 did not permeabilize the inner membrane of S. aureus. Gel retardation and circular dichroism spectra showed that Lfcin4 and Lfcin5 bound to bacterial genomic DNA. Lfcin4 inhibited DNA, RNA and protein synthesis. Both peptides induced the peeling of membranes and the lysis of S. enteritidis. At doses of 10 and 15 mg/kg, Lfcin4 and Lfcin5 reduced the bacterial counts in infected thigh muscles by 0.03‒0.10 and 0.05‒0.63 log10 CFU/g of tissue, respectively, within 10 h. Lfcin4 and Lfcin5 enhanced the survival rate of endotoxemic mice; reduced serum IL-6, IL-1β and TNF-α levels; and protected mice from lipopolysaccharide-induced lung injury. These data suggest that Lfcin4 and Lfcin5 may be antimicrobial and anti-endotoxin peptides that could serve as the basis for the development of dual-function agents.

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“…Rosenberger et al reported that in vitro incubation of Salmonella enterica serovar Typhimurium with sublethal levels of mouse cathelicidin-related antimicrobial peptide (CRAMP) causes the bacterial cell to become filamentous in shape with arrested septum formation (19). Li et al also found that the peptide-treated cells are unable to undergo cell division (31). In the current study, we found that, solely under aerobic growth conditions, the lengths of bacterial cells increased proportionally to the concentration of arabinose, which corresponds to the levels of intracellular expression of LL-37.This suggests that the increased cell length is particularly associated with the presence of free radicals, which are produced by intracellular LL-37 in the presence of oxygen.…”

Section: Discussionmentioning

confidence: 99%

“…In fact, the degree of membrane depolarization has been used as an assessing index for AMP efficacy (28). Since LL-37 is a cationic peptide, disruption of the cell membrane has been proposed as the primary mode of action for positively charged AMPs from outside (31,32).…”

Section: Discussionmentioning

confidence: 99%

Effect of Intracellular Expression of Antimicrobial Peptide LL-37 on Growth of Escherichia coli Strain TOP10 under Aerobic and Anaerobic Conditions

Liu

Dong

et al. 2013

Antimicrob Agents Chemother

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Antimicrobial peptides (AMPs) can cause lysis of target bacteria by directly inserting themselves into the lipid bilayer. This killing mechanism confounds the identification of the intracellular targets of AMPs. To circumvent this, we used a shuttle vector containing the inducible expression of a human cathelicidin-related AMP, LL-37, to examine its effect on Escherichia coli TOP10 under aerobic and anaerobic growth conditions. Induction of LL-37 caused growth inhibition and alteration in cell morphology to a filamentous phenotype. Further examination of the E. coli cell division protein FtsZ revealed that LL-37 did not interact with FtsZ. Moreover, intracellular expression of LL-37 results in the enhanced production of reactive oxygen species (ROS), causing lethal membrane depolarization under aerobic conditions. Additionally, the membrane permeability was increased after intracellular expression of LL37 under both aerobic and anaerobic conditions. Transcriptomic analysis revealed that intracellular LL-37 mainly affected the expression of genes related to energy production and carbohydrate metabolism. More specifically, genes related to oxidative phosphorylation under both aerobic and anaerobic growth conditions were affected. Collectively, our current study demonstrates that intracellular expression of LL-37 in E. coli can inhibit growth under aerobic and anaerobic conditions. While we confirmed that the generation of ROS is a bactericidal mechanism for LL-37 under aerobic growth conditions, we also found that the intracellular accumulation of cationic LL-37 influences the redox and ion status of the cells under both growth conditions. These data suggest that there is a new AMP-mediated bacterial killing mechanism that targets energy metabolism.

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Selectivity for and destruction of Salmonella typhimurium via a membrane damage mechanism of a cell-penetrating peptide ppTG20 analogue

Cited by 49 publications

References 30 publications

Cell Penetrating Peptides and Cationic Antibacterial Peptides

Cell Penetrating Peptides and Cationic Antibacterial Peptides

Killing of Staphylococcus aureus and Salmonella enteritidis and neutralization of lipopolysaccharide by 17-residue bovine lactoferricins: improved activity of Trp/Ala-containing molecules

Effect of Intracellular Expression of Antimicrobial Peptide LL-37 on Growth of Escherichia coli Strain TOP10 under Aerobic and Anaerobic Conditions

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