ArticlePloS one2015
OmpA Binding Mediates the Effect of Antimicrobial Peptide LL-37 on Acinetobacter baumannii.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 40 citations in OpenAlex.
- Article
- Inside Enemy Lines: Adhesion, Invasion, and Intracellular Persistence ofPathogens (Basel, Switzerland) · 2026Review
- AbOmpA in Acinetobacter baumannii: exploring virulence mechanisms of outer membrane-integrated and outer membrane vesicle-associated AbOmpA and developing anti-infective agents targeting AbOmpA.Journal of biomedical science · 2025Review
- Antimicrobial peptides: from discovery to developmental applications.Applied and environmental microbiology · 2025Review
- Natural peptides and their synthetic congeners acting againstRSC medicinal chemistry · 2025Review
- Famotidine Enhances Rifampicin Activity against Acinetobacter baumannii by Affecting OmpA.Journal of bacteriology · 2023Article
- The Tol-Pal system of Acinetobacter baumannii is important for cell morphology, antibiotic resistance and virulence.International microbiology : the official journal of the Spanish Society for Microbiology · 2023Article
- Antibiofilm properties of cathelicidin LL-37: an in-depth review.World journal of microbiology & biotechnology · 2023Review
- Association between Pneumonia Development and Virulence Gene Expression in Carbapenem-ResistantThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2023Article
- The Evolutionary History of Peptidases Involved in the Processing of Organelle-Targeting Peptides.Genome biology and evolution · 2022Article
- Mammals' humoral immune proteins and peptides targeting the bacterial envelope: from natural protection to therapeutic applications against multidrug-resistant Gram-negatives.Biological reviews of the Cambridge Philosophical Society · 2022Review
- The effects of LL-37 on virulence factors related to the quorum sensing system ofAnnals of translational medicine · 2022Article
- Clinical Isolates ofFrontiers in immunology · 2022Article
- Gram-Negative Bacteria Holding Together in a Biofilm: TheMicroorganisms · 2021Review
- Carboxy-Terminal Processing Protease Controls Production of Outer Membrane Vesicles and Biofilm inMicroorganisms · 2021Article
- The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent.Antibiotics (Basel, Switzerland) · 2021Review
- Genotypic and Phenotypic Characterization of Novel Sequence Types of Carbapenem-ResistantFrontiers in microbiology · 2021Article
- Mechanisms ProtectingInternational journal of molecular sciences · 2020Review
- Microevolution in the major outer membrane protein OmpA ofMicrobial genomics · 2020Article
- Outer membrane protein A (OmpA) as a potential therapeutic target for Acinetobacter baumannii infection.Journal of biomedical science · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multidrug-resistant Acinetobacter baumannii has recently emerged as an important pathogen in nosocomial infection; thus, effective antimicrobial regimens are urgently needed. Human antimicrobial peptides (AMPs) exhibit multiple functions and antimicrobial activities against bacteria and fungi and are proposed to be potential adjuvant therapeutic agents. This study examined the effect of the human cathelicidin-derived AMP LL-37 on A. baumannii and revealed the underlying mode of action. We found that LL-37 killed A. baumannii efficiently and reduced cell motility and adhesion. The bacteria-killing effect of LL-37 on A. baumannii was more efficient compared to other AMPs, including human ß-defensin 3 (hBD3) and histatin 5 (Hst5). Both flow cytometric analysis and immunofluorescence staining showed that LL-37 bound to A. baumannii cells. Moreover, far-western analysis demonstrated that LL-37 could bind to the A. baumannii OmpA (AbOmpA) protein. An ELISA assay indicated that biotin-labelled LL-37 (BA-LL37) bound to the AbOmpA74-84 peptide in a dose-dependent manner. Using BA-LL37 as a probe, the ~38 kDa OmpA signal was detected in the wild type but the ompA deletion strain did not show the protein, thereby validating the interaction. Finally, we found that the ompA deletion mutant was more sensitive to LL-37 and decreased cell adhesion by 32% compared to the wild type. However, ompA deletion mutant showed a greatly reduced adhesion defect after LL-37 treatment compared to the wild strain. Taken together, this study provides evidence that LL-37 affects A. baumannii through OmpA binding.
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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.