Observational studyMedicine2018
A bovine myeloid antimicrobial peptide (BMAP-28) and its analogs kill pan-drug-resistant Acinetobacter baumannii by interacting with outer membrane protein A (OmpA).
Observational study in Medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Design and TAG-Assisted Synthesis of the C-Terminal Amidated Antimicrobial Peptide NCBP-1 Derived from a Plant-Derived Noncanonical NCBP and Its Biological Activity.Protein and peptide letters · 2026Article
- Antimicrobial Peptides Versus Antibiotics in Farm Animal Production.Antibiotics (Basel, Switzerland) · 2025Review
- 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
- Designing of a novel chimeric antimicrobial peptide againstResearch in pharmaceutical sciences · 2025Article
- Natural peptides and their synthetic congeners acting againstRSC medicinal chemistry · 2025Review
- Current treatment strategies for targeting virulence factors and biofilm formation inFuture microbiology · 2024Review
- 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
- 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
- PaP1, a Broad-Spectrum Lysin-Derived Cationic Peptide to Treat Polymicrobial Skin Infections.Frontiers in microbiology · 2022Article
- Multidrug-Resistant Microbial Therapy Using Antimicrobial Peptides and the CRISPR/Cas9 System.Veterinary medicine (Auckland, N.Z.) · 2022Review
- Virulence Potential and Treatment Options of Multidrug-Resistant (MDR)Microorganisms · 2021Review
- A Study on the Antimicrobial and Antibiofilm Peptide 1018-K6 as Potential Alternative to Antibiotics against Food-PathogenFoods (Basel, Switzerland) · 2021Article
- Antimicrobial Peptides in Farm Animals: An Updated Review on Its Diversity, Function, Modes of Action and Therapeutic Prospects.Veterinary sciences · 2020Review
- Emerging Strategies to Combat β-Lactamase Producing ESKAPE Pathogens.International journal of molecular sciences · 2020Review
- Outcomes and prognostic factors of tigecycline treatment for hospital-acquired pneumonia involving multidrug-resistantThe Journal of international medical research · 2020Article
- Review
- Outer membrane protein A (OmpA) as a potential therapeutic target for Acinetobacter baumannii infection.Journal of biomedical science · 2020Review
- The Outer Membrane Proteins OmpA, CarO, and OprD ofFrontiers in microbiology · 2020Review
- Antimicrobial peptides: new hope in the war against multidrug resistance.Zoological research · 2019Review
- The antimicrobial peptides and their potential clinical applications.American journal of translational research · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial peptides (AMPs) exhibit multiple activities against bacteria and fungi. A bovine myeloid antimicrobial peptide (BMAP-28) belongs to the cathelicidin-derived AMPs and has antimicrobial activity. Due to the rapidly increasing number of infections and outbreaks caused by pan-drug-resistant Acinetobacter baumannii (PDRAB), we sought to determine whether BMAP-28 and its 4 analog peptides (A837, A838, A839, and A840) have antimicrobial activity against PDRAB. Furthermore, we clarified the possible mechanism of inhibition by which of BMAP-28 acts against PDRAB. In the current study, we examined the inhibitory effect of BMAP-28 and its 4 analog peptides on the growth of PDRAB through minimal inhibitory concentration (MIC) analysis and short time killing assays. We also evaluated the effects of BMAP-28 and its analogs on the bacterial cell surface through the use of field emission scanning electron microscopy (FE-SEM). In order to determine the inhibitory mechanism of BMAP-28, we examined the interaction between BMAP-28 and outer membrane proteins (OMPs), especially the interaction between BMAP-28 and A. baumannii OmpA (AbOmpA), which is the main component of OMPs, by using a quartz crystal microbalance (QCM). BMAP-28 and its 4 analogs were effective in inhibiting the growth of PDRAB and had rapid killing ability. BMAP-28 showed exceptionally strong and rapid inhibitory effects on PDRAB when compared to the other peptides and was also shown to cause damage to the cell surface of PDRAB. Moreover, QCM analysis provided evidence of potential interaction between BMAP-28 and AbOmpA. These data indicate that BMAP-28 is a promising candidate for the treatment of PDRAB infections and that its inhibitory effects were related with its binding to AbOmpA.
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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.