ArticleThe Journal of biological chemistry2015
Lipopolysaccharide Phosphorylation by the WaaY Kinase Affects the Susceptibility of Escherichia coli to the Human Antimicrobial Peptide LL-37.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 40 citations in OpenAlex.
- Overcoming LPS-mediated resistance in gram-negative pathogens: a review of LL-37 analogs and computational design strategies.Archives of microbiology · 2026Review
- Only time will tell: lipopolysaccharide glycoform and biofilm-formation kinetics inJournal of bacteriology · 2024Review
- Multiple resistance factors collectively promote inoculum-dependent dynamic survival during antimicrobial peptide exposure in Enterobacter cloacae.PLoS pathogens · 2024Article
- Multiple resistance factors collectively promote inoculum-dependent dynamic survival during antimicrobial peptide exposure inbioRxiv : the preprint server for biology · 2024Article
- Article
- Two homologous Salmonella serogroup C1-specific genes are required for flagellar motility and cell invasion.BMC genomics · 2021Article
- The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent.Antibiotics (Basel, Switzerland) · 2021Review
- Structural Plasticity of LL-37 Indicates Elaborate Functional Adaptation Mechanisms to Bacterial Target Structures.International journal of molecular sciences · 2021Review
- Cathelicidin-mediated lipopolysaccharide signaling via intracellular TLR4 in colonic epithelial cells evokes CXCL8 production.Gut microbes · 2020Article
- The Human Salivary Antimicrobial Peptide Profile according to the Oral Microbiota in Health, Periodontitis and Smoking.Journal of innate immunity · 2019Article
- Tuneable poration: host defense peptides as sequence probes for antimicrobial mechanisms.Scientific reports · 2018Article
- Bioinspired Designs, Molecular Premise and Tools for Evaluating the Ecological Importance of Antimicrobial Peptides.Pharmaceuticals (Basel, Switzerland) · 2018Review
- Antibiotic-resistant bacteria show widespread collateral sensitivity to antimicrobial peptides.Nature microbiology · 2018Article
- The Role of Outer Membrane Proteins and Lipopolysaccharides for the Sensitivity ofFrontiers in microbiology · 2018Article
- Membrane-Active Epithelial Keratin 6A Fragments (KAMPs) Are Unique Human Antimicrobial Peptides with a Non-αβ Structure.Frontiers in microbiology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human cathelicidin LL-37 is a multifunctional host defense peptide with immunomodulatory and antimicrobial roles. It kills bacteria primarily by altering membrane barrier properties, although the exact sequence of events leading to cell lysis has not yet been completely elucidated. Random insertion mutagenesis allowed isolation of Escherichia coli mutants with altered susceptibility to LL-37, pointing to factors potentially relevant to its activity. Among these, inactivation of the waaY gene, encoding a kinase responsible for heptose II phosphorylation in the LPS inner core, leads to a phenotype with decreased susceptibility to LL-37, stemming from a reduced amount of peptide binding to the surface of the cells, and a diminished capacity to lyse membranes. This points to a specific role of the LPS inner core in guiding LL-37 to the surface of Gram-negative bacteria. Although electrostatic interactions are clearly relevant, the susceptibility of the waaY mutant to other cationic helical cathelicidins was unaffected, indicating that particular structural features or LL-37 play a role in this interaction.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.