ArticleInfection and immunity1998
The lipopolysaccharide of Bordetella bronchiseptica acts as a protective shield against antimicrobial peptides.
Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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.
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Who cites it
34 citing papers in PubMed, 96 citations in OpenAlex.
- First inhibitor of a bacterial two-partner secretion system.bioRxiv : the preprint server for biology · 2026Article
- Latroeggtoxin-VI improves depression by regulating the composition and function of gut microbiota in a mouse model of depression.Journal of medical microbiology · 2025Article
- Single-Molecule-Level Quantification Based on Atomic Force Microscopy Data Reveals the Interaction between Melittin and Lipopolysaccharide in Gram-Negative Bacteria.International journal of molecular sciences · 2024Article
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- Repeat-Unit Elongations To Produce Bacterial Complex Long Polysaccharide Chains, an O-Antigen Perspective.EcoSal Plus · 2023Review
- Article
- Bacterial resistance to antibacterial agents: Mechanisms, control strategies, and implications for global health.The Science of the total environment · 2023Review
- Bps polysaccharide of Bordetella pertussis resists antimicrobial peptides by functioning as a dual surface shield and decoy and converts Escherichia coli into a respiratory pathogen.PLoS pathogens · 2022Article
- Article
- Qualitative and Quantitative Changes toLangmuir : the ACS journal of surfaces and colloids · 2020Article
- Effects of the Antimicrobial Peptide LL-37 and Innate Effector Mechanisms in Colistin-ResistantFrontiers in microbiology · 2019Article
- What we may expect from novel antibacterial agents in the pipeline with respect to resistance and pharmacodynamic principles.Journal of pharmacokinetics and pharmacodynamics · 2017Review
- Mutations in Novel Lipopolysaccharide Biogenesis Genes Confer Resistance to Amoebal Grazing in Synechococcus elongatus.Applied and environmental microbiology · 2016Article
- Antimicrobial Peptides from Fruits and Their Potential Use as Biotechnological Tools-A Review and Outlook.Frontiers in microbiology · 2016Review
- Antimicrobial peptide resistance in Neisseria meningitidis.Biochimica et biophysica acta · 2015Review
- Coevolution with bacteriophages drives genome-wide host evolution and constrains the acquisition of abiotic-beneficial mutations.Molecular biology and evolution · 2015Article
- Bordetella pertussis lipid A glucosamine modification confers resistance to cationic antimicrobial peptides and increases resistance to outer membrane perturbation.Antimicrobial agents and chemotherapy · 2014Article
- D-alanine modification of a protease-susceptible outer membrane component by the Bordetella pertussis dra locus promotes resistance to antimicrobial peptides and polymorphonuclear leukocyte-mediated killing.Journal of bacteriology · 2013Article
- Mechanisms of intrinsic resistance to antimicrobial peptides of Edwardsiella ictaluri and its influence on fish gut inflammation and virulence.Microbiology (Reading, England) · 2013Article
- Both group 4 capsule and lipopolysaccharide O-antigen contribute to enteropathogenic Escherichia coli resistance to human α-defensin 5.PloS one · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resistance profiles of the two Bordetella species B. bronchiseptica and B. pertussis against various antimicrobial peptides were determined in liquid survival and agar diffusion assays. B. bronchiseptica exhibited significantly higher resistance against all tested peptides than B. pertussis. The most powerful agents acting on B. bronchiseptica were, in the order of their killing efficiencies, cecropin P > cecropin B > magainin-II-amide > protamine > melittin. Interestingly, for B. bronchiseptica, the resistance level was significantly affected by phase variation, as a bvgS deletion derivative showed an increased sensitivity to these peptides. Tn5-induced protamine-sensitive B. bronchiseptica mutants, which were found to be very susceptible to most of the cationic peptides, were isolated. In two of these mutants, the genetic loci inactivated by transposon insertion were identified as containing genes highly homologous to the wlbA and wlbL genes of B. pertussis that are involved in the biosynthesis of lipopolysaccharide (LPS). In agreement with this finding, the two peptide-sensitive mutants revealed structural changes in the LPS, resulting in the loss of the O-specific side chains and the prevalence of the LPS core structure. This demonstrates that LPS plays a major role in the resistance of B. bronchiseptica against the action of antimicrobial peptides and suggests that B. pertussis is much more susceptible to these peptides due to the lack of the highly charged O-specific sugar side chains.
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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.