ArticleAntimicrobial agents and chemotherapy2008
Resistance of Porphyromonas gingivalis ATCC 33277 to direct killing by antimicrobial peptides is protease independent.
Article in Antimicrobial agents and chemotherapy, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed, 44 citations in OpenAlex.
- Natural and synthetic antimicrobial peptides against anaerobic bacteria: A review of activities and mechanisms of action.Probiotics and antimicrobial proteins · 2026Review
- Forging a New Frontier: Antimicrobial Peptides and Nanotechnology Converging to Conquer Gastrointestinal Pathogens.Small (Weinheim an der Bergstrasse, Germany) · 2025Review
- Review
- Review
- Effect of Fecal Microbiota Transplant on Antibiotic Resistance Genes Among Patients with Chronic Pouchitis.Digestive diseases and sciences · 2025Observational
- Understanding the Dynamics of Human Defensin Antimicrobial Peptides: Pathogen Resistance and Commensal Induction.Applied biochemistry and biotechnology · 2024Review
- The oral pathogen Porphyromonas gingivalis gains tolerance to the antimicrobial peptide DGL13K by synonymous mutations in hagA.PloS one · 2024Article
- Cathelicidin LL-37 in Health and Diseases of the Oral Cavity.Biomedicines · 2022Review
- Plasma treatment effects on destruction and recovery of Porphyromonas gingivalis biofilms.PloS one · 2022Article
- Interactions of two enantiomers of a designer antimicrobial peptide with structural components of the bacterial cell envelope.Journal of peptide science : an official publication of the European Peptide Society · 2022Article
- LL-37-Induced Autophagy Contributed to the Elimination of LiveFrontiers in cellular and infection microbiology · 2020Article
- Peptide and non-peptide mimetics as potential therapeutics targeting oral bacteria and oral biofilms.Molecular oral microbiology · 2019Review
- Potential Oral Health Care Agent from Coffee Against Virulence Factor of Periodontitis.Nutrients · 2019Article
- Anaerobic bacteria growth in the presence of cathelicidin LL-37 and selected ceragenins delivered as magnetic nanoparticles cargo.BMC microbiology · 2017Article
- Vaccination with recombinant RgpA peptide protects against Porphyromonas gingivalis-induced bone loss.Journal of periodontal research · 2017Article
- Experimental Induction of Bacterial Resistance to the Antimicrobial Peptide Tachyplesin I and Investigation of the Resistance Mechanisms.Antimicrobial agents and chemotherapy · 2016Article
- Bacterial Evasion of Host Antimicrobial Peptide Defenses.Microbiology spectrum · 2016Review
- P. gingivalis in Periodontal Disease and Atherosclerosis - Scenes of Action for Antimicrobial Peptides and Complement.Frontiers in immunology · 2015Review
- Actin enables the antimicrobial action of LL-37 peptide in the presence of microbial proteases.The Journal of biological chemistry · 2014Article
- Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance.Frontiers in microbiology · 2013Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Antimicrobial peptides are short, positively charged, amphipathic peptides that possess a wide spectrum of antimicrobial activity and have an important role in the host's innate immunity. Lack of, or dysfunctions in, antimicrobial peptides have been correlated with infectious diseases, including periodontitis. Porphyromonas gingivalis, a gram-negative anaerobe and a major pathogen associated with periodontal diseases, is resistant to antimicrobial peptides of human and nonhuman origin, a feature that likely contributes to its virulence. Expressing a robust proteolytic activity, P. gingivalis hydrolyzes antimicrobial peptides. In this study, P. gingivalis inactivated three antimicrobial peptides, while a d-enantiomer was resistant to degradation. P. gingivalis was resistant to the protease-resistant d-enantiomer peptide, and importantly, a protease-deficient P. gingivalis mutant was also resistant to the antimicrobial peptide. Finally, the binding of a fluorescently labeled antimicrobial peptide to protease-deficient P. gingivalis was much weaker than the binding of susceptible Escherichia coli. Our results suggest that the resistance of P. gingivalis ATCC 33277 to direct killing by antimicrobial peptides is protease independent and results (at least partially) from the low affinity of antimicrobial peptides to P. gingivalis.
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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.