ArticleBiochimica et biophysica acta. Biomembranes2019
Resistance of early stationary phase E. coli to membrane permeabilization by the antimicrobial peptide Cecropin A.
Article in Biochimica et biophysica acta. Biomembranes, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 30 citations in OpenAlex.
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- Optimizing Intracellular Transport of Antimicrobial Metallohelices Delivers Selective Nanomolar Potency inInorganic chemistry · 2026Article
- Antimicrobial peptide LL37 is potent against non-growingmSphere · 2025Article
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- Evaluation of Novel HLM Peptide Activity and Toxicity against Planktonic and Biofilm Bacteria: Comparison to Standard Antibiotics.Current protein & peptide science · 2024Article
- Expression of RcrB confers resistance to hypochlorous acid in uropathogenicJournal of bacteriology · 2023Article
- Expression of RcrB confers resistance to hypochlorous acid in uropathogenicbioRxiv : the preprint server for biology · 2023Article
- Sensitization of KPC and NDM Klebsiella pneumoniae To Rifampicin by the Human Lactoferrin-Derived Peptide hLF1-11.Microbiology spectrum · 2023Article
- Inoculum Concentration Influences Pseudomonas aeruginosa Phenotype and Biofilm Architecture.Microbiology spectrum · 2022Article
- Octenidine's Efficacy: A Matter of Interpretation or the Influence of Experimental Setups?Antibiotics (Basel, Switzerland) · 2022Article
- Polyimidazolium Protects against an Invasive Clinical Isolate of Salmonella Typhimurium.Antimicrobial agents and chemotherapy · 2022Article
- Multi-Omic Analysis to Characterize Metabolic Adaptation of theMetabolites · 2022Article
- Binding of cationic analogues of α-MSH to lipopolysaccharide and disruption of the cytoplasmic membranes caused bactericidal action against Escherichia coli.Scientific reports · 2022Article
- Bacteria Modify Their Sensitivity to Chemerin-Derived Peptides by Hindering Peptide Association With the Cell Surface and Peptide Oxidation.Frontiers in microbiology · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Antimicrobial peptides (AMPs) cause bacterial membrane permeabilization and ultimately cell death at low μM concentrations. The membrane permeabilization action of a moth derived AMP Cecropin A on E. coli cells in exponential growth (mid-log phase) is well studied. At 1× MIC concentration, Cecropin A penetrates the lipopolysaccharide (LPS) barrier and causes outer membrane (OM) and cytoplasmic membrane (CM) permeabilization. For non-septating cells, permeabilization of both membranes begins at one pole. For septating cells, OM permeabilization begins at the septal region and CM permeabilization begins at one pole. However, in nature bacteria are frequently found in nutrient-starved conditions. Here we extend our single-cell microscopy assays to the attack of Cecropin A on E. coli cells in early stationary phase. Stationary phase E. coli is much more resistant to membrane permeabilization by Cecropin A than mid-log phase E. coli. A tenfold higher concentration of Cecropin A is required to observe CM permeabilization in the majority of stationary phase cells, and even then permeabilization proceeds more slowly. In addition, the spatial pattern of initial CM permeabilization changes from localized at one pole to global. Studies of lipid mutant strains suggest that a sufficient localized concentration of the anionic phospholipid phosphatidylglycerol (PG) guides the position of initial attack of the cationic AMP Cecropin A on the CM.
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